Structural basis of GDP release and gating in G protein coupled Fe2+ transport
G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe 2+ transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the s...
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| Published in | The EMBO journal Vol. 28; no. 17; pp. 2677 - 2685 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
02.09.2009
Nature Publishing Group UK Springer Nature B.V Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0261-4189 1460-2075 1460-2075 |
| DOI | 10.1038/emboj.2009.208 |
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| Abstract | G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe
2+
transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide‐binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes. |
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| AbstractList | G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes. G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes. [PUBLICATION ABSTRACT] G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe 2+ transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes. G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe2+ transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide‐binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes. G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes.G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes. |
| Author | Guilfoyle, Amy Maher, Megan J Rapp, Mikaela Jormakka, Mika Clarke, Ronald Harrop, Stephen |
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| Cites_doi | 10.1126/SCIENCE.1062023 10.1107/S0907444994003112 10.1021/bi061088h 10.1126/science.3136547 10.1038/nature07330 10.1038/nature03018 10.1038/371164a0 10.1107/S0021889807021206 10.1124/mol.107.034348 10.1126/science.1085028 10.1073/pnas.242338299 10.1016/S0006-3495(93)81293-1 10.1073/pnas.0702623104 10.1038/nsmb1129 10.1074/jbc.M604867200 10.1107/S0907444996012255 10.1107/S0907444903017694 10.1038/nrm2299 10.1007/978-1-60327-058-8_28 10.1038/nature07462 10.1107/S0108767307043930 10.1007/s10534-006-0003-2 10.1126/science.1109730 10.1016/S0966-842X(03)00100-8 10.1016/0092-8674(95)90220-1 10.1093/nar/gkm216 10.1146/annurev.biochem.66.1.639 10.1016/S0092-8674(00)81212-X 10.1016/j.cell.2004.10.030 10.1016/j.jmb.2007.11.027 10.1126/science.1127121 10.1038/nrm2438 10.1073/pnas.0608599104 10.1126/science.1118890 10.1038/374378a0 10.1073/pnas.081441398 10.1038/nrm2646 10.1038/349117a0 10.1016/j.sbi.2007.07.003 10.1107/S0108767390010224 10.1107/S0907444904019158 10.1016/j.cellsig.2008.04.012 |
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| Copyright | European Molecular Biology Organization 2009 Copyright © 2009 European Molecular Biology Organization Copyright Nature Publishing Group Sep 2, 2009 Copyright © 2009, European Molecular Biology Organization 2009 |
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| Keywords | crystallography GDP release iron transport GTPase |
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| Notes | Supplementary Figure S1Supplementary Figure S2Supplementary Figure S3Supplementary Figure S4Supplementary Figure S5Supplementary Figure S6Supplementary Figure LegendsSupplementary InformationReview Process File ark:/67375/WNG-NZDP21GW-Q istex:0B3B9A149B1EF75A594538A9CC16703BF189F5B4 ArticleID:EMBJ2009208 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Present address: Division of Biophysics, Department of Medical Biochemistry and Biophysics, Karolinska Institute, 171 77 Stockholm, Sweden These authors contributed equally to this work |
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| References | Iiri T, Herzmark P, Nakamoto JM, van Dop C, Bourne HR (1994) Rapid GDP release from Gs alpha in patients with gain and loss of endocrine function. Nature 371: 164-168 Zwart PH, Afonine PV, Grosse-Kunstleve RW, Hung LW, Ioerger TR, McCoy AJ, McKee E, Moriarty NW, Read RJ, Sacchettini JC, Sauter NK, Storoni LC, Terwilliger TC, Adams PD (2008) Automated structure solution with the PHENIX suite. Methods Mol Biol 426: 419-435 Leslie AGW (1992) Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ ESF-EAMCB Newslett Protein Crystallogr 26: 11-20 Finlin BS, Correll RN, Pang C, Crump SM, Satin J, Andres DA (2006) Analysis of the complex between Ca2+ channel beta-subunit and the Rem GTPase. J Biol Chem 281: 23557-23566 Cachero TG, Morielli AD, Peralta EG (1998) The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel. Cell 93: 1077-1085 Oldham WM, Van Eps N, Preininger AM, Hubbell WL, Hamm HE (2007) Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteins. Proc Natl Acad Sci USA 104: 7927-7932 Sprang SR, Chen Z, Du X (2007) Structural basis of effector regulation and signal termination in heterotrimeric G[alpha] proteins. In Mechanisms and Pathways of Heterotrimeric G Protein Signaling, Sprang SR (ed) pp 1-65. San Diego: Academic Press Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr D Biol Crystallogr 59: 2023-2030 Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308: 1321-1323 Spoerner M, Herrmann C, Vetter IR, Kalbitzer HR, Wittinghofer A (2001) Dynamic properties of the Ras switch I region and its importance for binding to effectors. Proc Natl Acad Sci USA 98: 4944-4949 Karnoub AE, Weinberg RA (2008) Ras oncogenes: split personalities. Nat Rev Mol Cell Biol 9: 517-531 Sheldrick GM (2008) A short history of SHELX. Acta Crystallogr A 64: 112-122 Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, Tesmer JJG (2005) Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex. Science 310: 1686-1690 Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krausz N, Choe H, Hofmann KP, Ernst OP (2008) Crystal structure of opsin in its G-protein-interacting conformation. Nature 455: 497-502 Cartron M, Maddocks S, Gillingham P, Craven C, Andrews S (2006) Feo-transport of ferrous iron into bacteria. BioMetals 19: 143-157 Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132 McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ (2007) Phaser crystallographic software. J Appl Crystallogr 40: 658-674 Marlovits TC, Haase W, Herrmann C, Aller SG, Unger VM (2002) The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria. Proc Natl Acad Sci USA 99: 16243-16248 Hamm HE, Deretic D, Arendt A, Hargrave PA, Koenig B, Hofmann KP (1988) Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit. Science 241: 832-835 Rees DC, Johnson E, Lewinson O (2009) ABC transporters: the power to change. Nat Rev Mol Cell Biol 10: 218-227 Oldham WM, Van Eps N, Preininger AM, Hubbell WL, Hamm HE (2006) Mechanism of the receptor-catalyzed activation of heterotrimeric G proteins. Nat Struct Mol Biol 13: 772-777 Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WB, Snoeyink J, Richardson JS, Richardson DC (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-W383 Eshaghi S, Niegowski D, Kohl A, Molina DM, Lesley SA, Nordlund P (2006) Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution. Science 313: 354-357 Oldham WM, Hamm HE (2007) How do receptors activate G proteins? In Mechanisms and Pathways of Heterotrimeric G Protein Signaling, Sprang SR (ed) pp 67-93. San Diego: Academic Press Oldham WM, Hamm HE (2008) Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol 9: 60-71 Sprang SR (1997) G protein mechanisms: insights from structural analysis. Annu Rev Biochem 66: 639-678 Johnston CA, Siderovski DP (2007a) Receptor-mediated activation of heterotrimeric G-proteins: current structural insights. Mol Pharmacol 72: 219-230 Vetter IR, Wittinghofer A (2001) The guanine nucleotide-binding switch in three dimensions. Science 294: 1299-1304 Wall MA, Coleman DE, Lee E, Iñiguez-Lluhi JA, Posner BA, Gilman AG, Sprang SR (1995) The structure of the G protein heterotrimer Gi[alpha]1[beta]1[gamma]2. Cell 83: 1047-1058 Bocquet N, Nury H, Baaden M, Le Poupon C, Changeux JP, Delarue M, Corringer PJ (2009) X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457: 111-114 Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH (2004) Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell 119: 615-627 Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53: 240-255 Yernool D, Boudker O, Jin Y, Gouaux E (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431: 811-818 Hollenstein K, Dawson RJ, Locher KP (2007) Structure and mechanism of ABC transporter proteins. Curr Opin Struct Biol 17: 412-418 Johnston CA, Siderovski DP (2007b) Structural basis for nucleotide exchange on Gαi subunits and receptor coupling specificity. Proc Natl Acad Sci 104: 2001-2006 Abdulaev NG, Ngo T, Ramon E, Brabazon DM, Marino JP, Ridge KD (2006) The receptor-bound 'empty pocket' state of the heterotrimeric G-protein alpha-subunit is conformationally dynamic. Biochemistry 45: 12986-12997 Hantke K (2003) Is the bacterial ferrous iron transporter FeoB a living fossil? Trends Microbiol 11: 192-195 Schaafsma D, Roscioni SS, Meurs H, Schmidt M (2008) Monomeric G-proteins as signal transducers in airway physiology and pathophysiology. Cell Signal 20: 1705-1714 Scheffzek K, Klebe C, Fritz-Wolf K, Kabsch W, Wittinghofer A (1995) Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature 374: 378-381 Kuo A, Gulbis JM, Antcliff JF, Rahman T, Lowe ED, Zimmer J, Cuthbertson J, Ashcroft FM, Ezaki T, Doyle DA (2003) Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300: 1922-1926 Eng ET, Jalilian AR, Spasov KA, Unger VM (2008) Characterization of a novel prokaryotic GDP dissociation inhibitor domain from the G protein coupled membrane protein FeoB. J Mol Biol 375: 1086-1097 Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47 (Pt 2): 110-119 Bourne HR, Sanders DA, McCormick F (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349: 117-127 Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763 Otwinowski Z, Minor W, Charles W, Carter J (1997) Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology Macromolecular Crystallography Part A, pp 307-326. San Diego: Academic Press Smart OS, Goodfellow JM, Wallace BA (1993) The pore dimensions of gramicidin A. Biophys J 65: 2455-2460 Spoerner, Herrmann, Vetter, Kalbitzer, Wittinghofer (CR39) 2001; 98 Vetter, Wittinghofer (CR43) 2001; 294 Oldham, Van Eps, Preininger, Hubbell, Hamm (CR30) 2006; 13 Cachero, Morielli, Peralta (CR5) 1998; 93 Eshaghi, Niegowski, Kohl, Molina, Lesley, Nordlund (CR13) 2006; 313 Iiri, Herzmark, Nakamoto, van Dop, Bourne (CR18) 1994; 371 Johnston, Siderovski (CR20) 2007; 104 Scheerer, Park, Hildebrand, Kim, Krausz, Choe, Hofmann, Ernst (CR35) 2008; 455 Hantke (CR16) 2003; 11 Clayton, Silverman, Heginbotham, Morais‐Cabral (CR7) 2004; 119 CR32 Abdulaev, Ngo, Ramon, Brabazon, Marino, Ridge (CR1) 2006; 45 Emsley, Cowtan (CR11) 2004; 60 Smart, Goodfellow, Wallace (CR38) 1993; 65 Davis, Leaver‐Fay, Chen, Block, Kapral, Wang, Murray, Arendall, Snoeyink, Richardson, Richardson (CR10) 2007; 35 Murshudov, Vagin, Dodson (CR27) 1997; 53 Cartron, Maddocks, Gillingham, Craven, Andrews (CR6) 2006; 19 Scheffzek, Klebe, Fritz‐Wolf, Kabsch, Wittinghofer (CR36) 1995; 374 Eng, Jalilian, Spasov, Unger (CR12) 2008; 375 Kuo, Gulbis, Antcliff, Rahman, Lowe, Zimmer, Cuthbertson, Ashcroft, Ezaki, Doyle (CR23) 2003; 300 Finlin, Correll, Pang, Crump, Satin, Andres (CR14) 2006; 281 Yernool, Boudker, Jin, Gouaux (CR45) 2004; 431 Bricogne, Vonrhein, Flensburg, Schiltz, Paciorek (CR4) 2003; 59 Daley, Rapp, Granseth, Melen, Drew, von Heijne (CR9) 2005; 308 Johnston, Siderovski (CR19) 2007; 72 Leslie (CR24) 1992; 26 Bocquet, Nury, Baaden, Le Poupon, Changeux, Delarue, Corringer (CR2) 2009; 457 Sheldrick (CR37) 2008; 64 Karnoub, Weinberg (CR22) 2008; 9 Wall, Coleman, Lee, Iñiguez‐Lluhi, Posner, Gilman, Sprang (CR44) 1995; 83 Tesmer, Kawano, Shankaranarayanan, Kozasa, Tesmer (CR42) 2005; 310 Oldham, Hamm (CR29) 2008; 9 CR8 CR28 Zwart, Afonine, Grosse‐Kunstleve, Hung, Ioerger, McCoy, McKee, Moriarty, Read, Sacchettini, Sauter, Storoni, Terwilliger, Adams (CR46) 2008; 426 Rees, Johnson, Lewinson (CR33) 2009; 10 McCoy, Grosse‐Kunstleve, Adams, Winn, Storoni, Read (CR26) 2007; 40 Jones, Zou, Cowan, Kjeldgaard (CR21) 1991; 47 Hamm, Deretic, Arendt, Hargrave, Koenig, Hofmann (CR15) 1988; 241 CR41 Oldham, Van Eps, Preininger, Hubbell, Hamm (CR31) 2007; 104 Schaafsma, Roscioni, Meurs, Schmidt (CR34) 2008; 20 Bourne, Sanders, McCormick (CR3) 1991; 349 Marlovits, Haase, Herrmann, Aller, Unger (CR25) 2002; 99 Sprang (CR40) 1997; 66 Hollenstein, Dawson, Locher (CR17) 2007; 17 2007; 17 2007; 104 2004; 60 1997; 66 2006; 13 2005; 310 1993; 65 1994; 371 2002; 99 2008; 9 2007a; 72 1997 2003; 59 2007 2008; 426 2006; 19 1988; 241 2007b; 104 1995; 374 2006; 313 2007; 35 2009; 457 2003; 11 2004; 431 1995; 83 2001; 294 1991; 47 2009; 10 2006; 45 1997; 53 2005; 308 1992; 26 2007; 40 2008; 455 1998; 93 2006; 281 2008; 20 2008; 64 1991; 349 2004; 119 2008; 375 1994; 50 2003; 300 2001; 98 emboj2009208-b20 emboj2009208-b42 emboj2009208-b41 emboj2009208-b22 emboj2009208-b44 emboj2009208-b21 Leslie AGW (emboj2009208-b24) 1992; 26 emboj2009208-b43 emboj2009208-b1 emboj2009208-b2 emboj2009208-b23 emboj2009208-b45 emboj2009208-b26 emboj2009208-b25 emboj2009208-b28 emboj2009208-b27 emboj2009208-b29 emboj2009208-b40 emboj2009208-b31 emboj2009208-b30 emboj2009208-b11 emboj2009208-b33 emboj2009208-b10 emboj2009208-b32 emboj2009208-b13 emboj2009208-b35 emboj2009208-b12 emboj2009208-b34 emboj2009208-b15 emboj2009208-b37 emboj2009208-b14 emboj2009208-b36 emboj2009208-b17 emboj2009208-b39 emboj2009208-b38 emboj2009208-b19 emboj2009208-b18 Zwart PH (emboj2009208-b46) 2008; 426 emboj2009208-b5 emboj2009208-b6 emboj2009208-b3 Hantke K (emboj2009208-b16) 2003; 11 emboj2009208-b4 emboj2009208-b9 emboj2009208-b7 emboj2009208-b8 |
| References_xml | – reference: Finlin BS, Correll RN, Pang C, Crump SM, Satin J, Andres DA (2006) Analysis of the complex between Ca2+ channel beta-subunit and the Rem GTPase. J Biol Chem 281: 23557-23566 – reference: Hantke K (2003) Is the bacterial ferrous iron transporter FeoB a living fossil? Trends Microbiol 11: 192-195 – reference: Otwinowski Z, Minor W, Charles W, Carter J (1997) Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology Macromolecular Crystallography Part A, pp 307-326. San Diego: Academic Press – reference: Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr D Biol Crystallogr 59: 2023-2030 – reference: Kuo A, Gulbis JM, Antcliff JF, Rahman T, Lowe ED, Zimmer J, Cuthbertson J, Ashcroft FM, Ezaki T, Doyle DA (2003) Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300: 1922-1926 – reference: Abdulaev NG, Ngo T, Ramon E, Brabazon DM, Marino JP, Ridge KD (2006) The receptor-bound 'empty pocket' state of the heterotrimeric G-protein alpha-subunit is conformationally dynamic. Biochemistry 45: 12986-12997 – reference: Schaafsma D, Roscioni SS, Meurs H, Schmidt M (2008) Monomeric G-proteins as signal transducers in airway physiology and pathophysiology. Cell Signal 20: 1705-1714 – reference: Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132 – reference: Rees DC, Johnson E, Lewinson O (2009) ABC transporters: the power to change. Nat Rev Mol Cell Biol 10: 218-227 – reference: Vetter IR, Wittinghofer A (2001) The guanine nucleotide-binding switch in three dimensions. Science 294: 1299-1304 – reference: Sprang SR, Chen Z, Du X (2007) Structural basis of effector regulation and signal termination in heterotrimeric G[alpha] proteins. In Mechanisms and Pathways of Heterotrimeric G Protein Signaling, Sprang SR (ed) pp 1-65. San Diego: Academic Press – reference: Eshaghi S, Niegowski D, Kohl A, Molina DM, Lesley SA, Nordlund P (2006) Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution. Science 313: 354-357 – reference: McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ (2007) Phaser crystallographic software. J Appl Crystallogr 40: 658-674 – reference: Sprang SR (1997) G protein mechanisms: insights from structural analysis. Annu Rev Biochem 66: 639-678 – reference: Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763 – reference: Sheldrick GM (2008) A short history of SHELX. Acta Crystallogr A 64: 112-122 – reference: Oldham WM, Van Eps N, Preininger AM, Hubbell WL, Hamm HE (2006) Mechanism of the receptor-catalyzed activation of heterotrimeric G proteins. Nat Struct Mol Biol 13: 772-777 – reference: Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53: 240-255 – reference: Wall MA, Coleman DE, Lee E, Iñiguez-Lluhi JA, Posner BA, Gilman AG, Sprang SR (1995) The structure of the G protein heterotrimer Gi[alpha]1[beta]1[gamma]2. Cell 83: 1047-1058 – reference: Spoerner M, Herrmann C, Vetter IR, Kalbitzer HR, Wittinghofer A (2001) Dynamic properties of the Ras switch I region and its importance for binding to effectors. Proc Natl Acad Sci USA 98: 4944-4949 – reference: Hollenstein K, Dawson RJ, Locher KP (2007) Structure and mechanism of ABC transporter proteins. Curr Opin Struct Biol 17: 412-418 – reference: Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH (2004) Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell 119: 615-627 – reference: Marlovits TC, Haase W, Herrmann C, Aller SG, Unger VM (2002) The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria. Proc Natl Acad Sci USA 99: 16243-16248 – reference: Zwart PH, Afonine PV, Grosse-Kunstleve RW, Hung LW, Ioerger TR, McCoy AJ, McKee E, Moriarty NW, Read RJ, Sacchettini JC, Sauter NK, Storoni LC, Terwilliger TC, Adams PD (2008) Automated structure solution with the PHENIX suite. Methods Mol Biol 426: 419-435 – reference: Bocquet N, Nury H, Baaden M, Le Poupon C, Changeux JP, Delarue M, Corringer PJ (2009) X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457: 111-114 – reference: Karnoub AE, Weinberg RA (2008) Ras oncogenes: split personalities. Nat Rev Mol Cell Biol 9: 517-531 – reference: Eng ET, Jalilian AR, Spasov KA, Unger VM (2008) Characterization of a novel prokaryotic GDP dissociation inhibitor domain from the G protein coupled membrane protein FeoB. J Mol Biol 375: 1086-1097 – reference: Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, Tesmer JJG (2005) Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex. Science 310: 1686-1690 – reference: Scheffzek K, Klebe C, Fritz-Wolf K, Kabsch W, Wittinghofer A (1995) Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature 374: 378-381 – reference: Smart OS, Goodfellow JM, Wallace BA (1993) The pore dimensions of gramicidin A. Biophys J 65: 2455-2460 – reference: Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WB, Snoeyink J, Richardson JS, Richardson DC (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-W383 – reference: Johnston CA, Siderovski DP (2007b) Structural basis for nucleotide exchange on Gαi subunits and receptor coupling specificity. Proc Natl Acad Sci 104: 2001-2006 – reference: Leslie AGW (1992) Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ ESF-EAMCB Newslett Protein Crystallogr 26: 11-20 – reference: Johnston CA, Siderovski DP (2007a) Receptor-mediated activation of heterotrimeric G-proteins: current structural insights. Mol Pharmacol 72: 219-230 – reference: Oldham WM, Hamm HE (2008) Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol 9: 60-71 – reference: Yernool D, Boudker O, Jin Y, Gouaux E (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431: 811-818 – reference: Hamm HE, Deretic D, Arendt A, Hargrave PA, Koenig B, Hofmann KP (1988) Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit. Science 241: 832-835 – reference: Oldham WM, Van Eps N, Preininger AM, Hubbell WL, Hamm HE (2007) Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteins. Proc Natl Acad Sci USA 104: 7927-7932 – reference: Cartron M, Maddocks S, Gillingham P, Craven C, Andrews S (2006) Feo-transport of ferrous iron into bacteria. BioMetals 19: 143-157 – reference: Iiri T, Herzmark P, Nakamoto JM, van Dop C, Bourne HR (1994) Rapid GDP release from Gs alpha in patients with gain and loss of endocrine function. Nature 371: 164-168 – reference: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308: 1321-1323 – reference: Oldham WM, Hamm HE (2007) How do receptors activate G proteins? In Mechanisms and Pathways of Heterotrimeric G Protein Signaling, Sprang SR (ed) pp 67-93. San Diego: Academic Press – reference: Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krausz N, Choe H, Hofmann KP, Ernst OP (2008) Crystal structure of opsin in its G-protein-interacting conformation. Nature 455: 497-502 – reference: Bourne HR, Sanders DA, McCormick F (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349: 117-127 – reference: Cachero TG, Morielli AD, Peralta EG (1998) The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel. Cell 93: 1077-1085 – reference: Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47 (Pt 2): 110-119 – volume: 98 start-page: 4944 year: 2001 end-page: 4949 ident: CR39 article-title: Dynamic properties of the Ras switch I region and its importance for binding to effectors publication-title: Proc Natl Acad Sci USA – volume: 457 start-page: 111 year: 2009 end-page: 114 ident: CR2 article-title: X‐ray structure of a pentameric ligand‐gated ion channel in an apparently open conformation publication-title: Nature – volume: 9 start-page: 60 year: 2008 end-page: 71 ident: CR29 article-title: Heterotrimeric G protein activation by G‐protein‐coupled receptors publication-title: Nat Rev Mol Cell Biol – volume: 13 start-page: 772 year: 2006 end-page: 777 ident: CR30 article-title: Mechanism of the receptor‐catalyzed activation of heterotrimeric G proteins publication-title: Nat Struct Mol Biol – volume: 45 start-page: 12986 year: 2006 end-page: 12997 ident: CR1 article-title: The receptor‐bound ‘empty pocket’ state of the heterotrimeric G‐protein alpha‐subunit is conformationally dynamic publication-title: Biochemistry – volume: 455 start-page: 497 year: 2008 end-page: 502 ident: CR35 article-title: Crystal structure of opsin in its G‐protein‐interacting conformation publication-title: Nature – volume: 53 start-page: 240 year: 1997 end-page: 255 ident: CR27 article-title: Refinement of macromolecular structures by the maximum‐likelihood method publication-title: Acta Crystallogr D Biol Crystallogr – volume: 426 start-page: 419 year: 2008 end-page: 435 ident: CR46 article-title: Automated structure solution with the PHENIX suite publication-title: Methods Mol Biol – volume: 281 start-page: 23557 year: 2006 end-page: 23566 ident: CR14 article-title: Analysis of the complex between Ca2+ channel beta‐subunit and the Rem GTPase publication-title: J Biol Chem – volume: 99 start-page: 16243 year: 2002 end-page: 16248 ident: CR25 article-title: The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria publication-title: Proc Natl Acad Sci USA – volume: 374 start-page: 378 year: 1995 end-page: 381 ident: CR36 article-title: Crystal structure of the nuclear Ras‐related protein Ran in its GDP‐bound form publication-title: Nature – volume: 308 start-page: 1321 year: 2005 end-page: 1323 ident: CR9 article-title: Global topology analysis of the Escherichia coli inner membrane proteome publication-title: Science – volume: 93 start-page: 1077 year: 1998 end-page: 1085 ident: CR5 article-title: The small GTP‐binding protein RhoA regulates a delayed rectifier potassium channel publication-title: Cell – volume: 119 start-page: 615 year: 2004 end-page: 627 ident: CR7 article-title: Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel publication-title: Cell – volume: 11 start-page: 192 year: 2003 end-page: 195 ident: CR16 article-title: Is the bacterial ferrous iron transporter FeoB a living fossil? publication-title: Trends Microbiol – volume: 40 start-page: 658 year: 2007 end-page: 674 ident: CR26 article-title: Phaser crystallographic software publication-title: J Appl Crystallogr – ident: CR8 – volume: 60 start-page: 2126 year: 2004 end-page: 2132 ident: CR11 article-title: Coot: model‐building tools for molecular graphics publication-title: Acta Crystallogr D Biol Crystallogr – volume: 17 start-page: 412 year: 2007 end-page: 418 ident: CR17 article-title: Structure and mechanism of ABC transporter proteins publication-title: Curr Opin Struct Biol – volume: 20 start-page: 1705 year: 2008 end-page: 1714 ident: CR34 article-title: Monomeric G‐proteins as signal transducers in airway physiology and pathophysiology publication-title: Cell Signal – volume: 65 start-page: 2455 year: 1993 end-page: 2460 ident: CR38 article-title: The pore dimensions of gramicidin A publication-title: Biophys J – volume: 83 start-page: 1047 year: 1995 end-page: 1058 ident: CR44 article-title: The structure of the G protein heterotrimer Gi[alpha]1[beta]1[gamma]2 publication-title: Cell – volume: 59 start-page: 2023 year: 2003 end-page: 2030 ident: CR4 article-title: Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0 publication-title: Acta Crystallogr D Biol Crystallogr – volume: 10 start-page: 218 year: 2009 end-page: 227 ident: CR33 article-title: ABC transporters: the power to change publication-title: Nat Rev Mol Cell Biol – volume: 9 start-page: 517 year: 2008 end-page: 531 ident: CR22 article-title: Ras oncogenes: split personalities publication-title: Nat Rev Mol Cell Biol – volume: 310 start-page: 1686 year: 2005 end-page: 1690 ident: CR42 article-title: Snapshot of activated G proteins at the membrane: the Galphaq‐GRK2‐Gbetagamma complex publication-title: Science – volume: 294 start-page: 1299 year: 2001 end-page: 1304 ident: CR43 article-title: The guanine nucleotide‐binding switch in three dimensions publication-title: Science – volume: 371 start-page: 164 year: 1994 end-page: 168 ident: CR18 article-title: Rapid GDP release from Gs alpha in patients with gain and loss of endocrine function publication-title: Nature – volume: 47 start-page: 110 year: 1991 end-page: 119 ident: CR21 article-title: Improved methods for building protein models in electron density maps and the location of errors in these models publication-title: Acta Crystallogr A – volume: 35 start-page: W375 year: 2007 end-page: W383 ident: CR10 article-title: MolProbity: all‐atom contacts and structure validation for proteins and nucleic acids publication-title: Nucleic Acids Res – volume: 313 start-page: 354 year: 2006 end-page: 357 ident: CR13 article-title: Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution publication-title: Science – volume: 104 start-page: 2001 year: 2007 end-page: 2006 ident: CR20 article-title: Structural basis for nucleotide exchange on Gαi subunits and receptor coupling specificity publication-title: Proc Natl Acad Sci – volume: 241 start-page: 832 year: 1988 end-page: 835 ident: CR15 article-title: Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit publication-title: Science – ident: CR32 – volume: 104 start-page: 7927 year: 2007 end-page: 7932 ident: CR31 article-title: Mapping allosteric connections from the receptor to the nucleotide‐binding pocket of heterotrimeric G proteins publication-title: Proc Natl Acad Sci USA – volume: 300 start-page: 1922 year: 2003 end-page: 1926 ident: CR23 article-title: Crystal structure of the potassium channel KirBac1.1 in the closed state publication-title: Science – volume: 431 start-page: 811 year: 2004 end-page: 818 ident: CR45 article-title: Structure of a glutamate transporter homologue from Pyrococcus horikoshii publication-title: Nature – volume: 349 start-page: 117 year: 1991 end-page: 127 ident: CR3 article-title: The GTPase superfamily: conserved structure and molecular mechanism publication-title: Nature – volume: 64 start-page: 112 year: 2008 end-page: 122 ident: CR37 article-title: A short history of SHELX publication-title: Acta Crystallogr A – volume: 72 start-page: 219 year: 2007 end-page: 230 ident: CR19 article-title: Receptor‐mediated activation of heterotrimeric G‐proteins: current structural insights publication-title: Mol Pharmacol – ident: CR28 – ident: CR41 – volume: 375 start-page: 1086 year: 2008 end-page: 1097 ident: CR12 article-title: Characterization of a novel prokaryotic GDP dissociation inhibitor domain from the G protein coupled membrane protein FeoB publication-title: J Mol Biol – volume: 66 start-page: 639 year: 1997 end-page: 678 ident: CR40 article-title: G protein mechanisms: insights from structural analysis publication-title: Annu Rev Biochem – volume: 26 start-page: 11 year: 1992 end-page: 20 ident: CR24 article-title: Recent changes to the MOSFLM package for processing film and image plate data publication-title: Joint CCP4+ ESF‐EAMCB Newslett Protein Crystallogr – volume: 19 start-page: 143 year: 2006 end-page: 157 ident: CR6 article-title: Feo—transport of ferrous iron into bacteria publication-title: BioMetals – volume: 349 start-page: 117 year: 1991 end-page: 127 article-title: The GTPase superfamily: conserved structure and molecular mechanism publication-title: Nature – volume: 93 start-page: 1077 year: 1998 end-page: 1085 article-title: The small GTP‐binding protein RhoA regulates a delayed rectifier potassium channel publication-title: Cell – volume: 241 start-page: 832 year: 1988 end-page: 835 article-title: Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit publication-title: Science – volume: 104 start-page: 2001 year: 2007b end-page: 2006 article-title: Structural basis for nucleotide exchange on Gαi subunits and receptor coupling specificity publication-title: Proc Natl Acad Sci – start-page: 67 year: 2007 end-page: 93 article-title: How do receptors activate G proteins publication-title: Mechanisms and Pathways of Heterotrimeric G Protein Signaling – volume: 99 start-page: 16243 year: 2002 end-page: 16248 article-title: The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria publication-title: Proc Natl Acad Sci USA – volume: 281 start-page: 23557 year: 2006 end-page: 23566 article-title: Analysis of the complex between Ca2+ channel beta‐subunit and the Rem GTPase publication-title: J Biol Chem – volume: 9 start-page: 60 year: 2008 end-page: 71 article-title: Heterotrimeric G protein activation by G‐protein‐coupled receptors publication-title: Nat Rev Mol Cell Biol – volume: 104 start-page: 7927 year: 2007 end-page: 7932 article-title: Mapping allosteric connections from the receptor to the nucleotide‐binding pocket of heterotrimeric G proteins publication-title: Proc Natl Acad Sci USA – volume: 50 start-page: 760 year: 1994 end-page: 763 article-title: The CCP4 suite: programs for protein crystallography publication-title: Acta Crystallogr D Biol Crystallogr – volume: 47 start-page: 110 year: 1991 end-page: 119 article-title: Improved methods for building protein models in electron density maps and the location of errors in these models publication-title: Acta Crystallogr A – volume: 65 start-page: 2455 year: 1993 end-page: 2460 article-title: The pore dimensions of gramicidin A publication-title: Biophys J – volume: 11 start-page: 192 year: 2003 end-page: 195 article-title: Is the bacterial ferrous iron transporter FeoB a living fossil? publication-title: Trends Microbiol – volume: 9 start-page: 517 year: 2008 end-page: 531 article-title: Ras oncogenes: split personalities publication-title: Nat Rev Mol Cell Biol – volume: 13 start-page: 772 year: 2006 end-page: 777 article-title: Mechanism of the receptor‐catalyzed activation of heterotrimeric G proteins publication-title: Nat Struct Mol Biol – volume: 20 start-page: 1705 year: 2008 end-page: 1714 article-title: Monomeric G‐proteins as signal transducers in airway physiology and pathophysiology publication-title: Cell Signal – volume: 10 start-page: 218 year: 2009 end-page: 227 article-title: ABC transporters: the power to change publication-title: Nat Rev Mol Cell Biol – volume: 371 start-page: 164 year: 1994 end-page: 168 article-title: Rapid GDP release from Gs alpha in patients with gain and loss of endocrine function publication-title: Nature – volume: 294 start-page: 1299 year: 2001 end-page: 1304 article-title: The guanine nucleotide‐binding switch in three dimensions publication-title: Science – volume: 119 start-page: 615 year: 2004 end-page: 627 article-title: Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel publication-title: Cell – volume: 431 start-page: 811 year: 2004 end-page: 818 article-title: Structure of a glutamate transporter homologue from Pyrococcus horikoshii publication-title: Nature – volume: 310 start-page: 1686 year: 2005 end-page: 1690 article-title: Snapshot of activated G proteins at the membrane: the Galphaq‐GRK2‐Gbetagamma complex publication-title: Science – volume: 26 start-page: 11 year: 1992 end-page: 20 article-title: Recent changes to the MOSFLM package for processing film and image plate data publication-title: Joint CCP4+ ESF‐EAMCB Newslett Protein Crystallogr – volume: 59 start-page: 2023 year: 2003 end-page: 2030 article-title: Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0 publication-title: Acta Crystallogr D Biol Crystallogr – volume: 19 start-page: 143 year: 2006 end-page: 157 article-title: Feo—transport of ferrous iron into bacteria publication-title: BioMetals – volume: 53 start-page: 240 year: 1997 end-page: 255 article-title: Refinement of macromolecular structures by the maximum‐likelihood method publication-title: Acta Crystallogr D Biol Crystallogr – volume: 375 start-page: 1086 year: 2008 end-page: 1097 article-title: Characterization of a novel prokaryotic GDP dissociation inhibitor domain from the G protein coupled membrane protein FeoB publication-title: J Mol Biol – start-page: 307 year: 1997 end-page: 326 article-title: Processing of X‐ray diffraction data collected in oscillation mode publication-title: Methods in Enzymology Macromolecular Crystallography Part A – volume: 457 start-page: 111 year: 2009 end-page: 114 article-title: X‐ray structure of a pentameric ligand‐gated ion channel in an apparently open conformation publication-title: Nature – start-page: 1 year: 2007 end-page: 65 article-title: Structural basis of effector regulation and signal termination in heterotrimeric G[alpha] proteins publication-title: Mechanisms and Pathways of Heterotrimeric G Protein Signaling – volume: 35 start-page: W375 year: 2007 end-page: W383 article-title: MolProbity: all‐atom contacts and structure validation for proteins and nucleic acids publication-title: Nucleic Acids Res – volume: 313 start-page: 354 year: 2006 end-page: 357 article-title: Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution publication-title: Science – volume: 17 start-page: 412 year: 2007 end-page: 418 article-title: Structure and mechanism of ABC transporter proteins publication-title: Curr Opin Struct Biol – volume: 64 start-page: 112 year: 2008 end-page: 122 article-title: A short history of SHELX publication-title: Acta Crystallogr A – volume: 98 start-page: 4944 year: 2001 end-page: 4949 article-title: Dynamic properties of the Ras switch I region and its importance for binding to effectors publication-title: Proc Natl Acad Sci USA – volume: 426 start-page: 419 year: 2008 end-page: 435 article-title: Automated structure solution with the PHENIX suite publication-title: Methods Mol Biol – volume: 83 start-page: 1047 year: 1995 end-page: 1058 article-title: The structure of the G protein heterotrimer Gi[alpha]1[beta]1[gamma]2 publication-title: Cell – volume: 66 start-page: 639 year: 1997 end-page: 678 article-title: G protein mechanisms: insights from structural analysis publication-title: Annu Rev Biochem – volume: 40 start-page: 658 year: 2007 end-page: 674 article-title: Phaser crystallographic software publication-title: J Appl Crystallogr – volume: 308 start-page: 1321 year: 2005 end-page: 1323 article-title: Global topology analysis of the Escherichia coli inner membrane proteome publication-title: Science – volume: 72 start-page: 219 year: 2007a end-page: 230 article-title: Receptor‐mediated activation of heterotrimeric G‐proteins: current structural insights publication-title: Mol Pharmacol – volume: 374 start-page: 378 year: 1995 end-page: 381 article-title: Crystal structure of the nuclear Ras‐related protein Ran in its GDP‐bound form publication-title: Nature – volume: 45 start-page: 12986 year: 2006 end-page: 12997 article-title: The receptor‐bound ‘empty pocket’ state of the heterotrimeric G‐protein alpha‐subunit is conformationally dynamic publication-title: Biochemistry – volume: 60 start-page: 2126 year: 2004 end-page: 2132 article-title: Coot: model‐building tools for molecular graphics publication-title: Acta Crystallogr D Biol Crystallogr – volume: 300 start-page: 1922 year: 2003 end-page: 1926 article-title: Crystal structure of the potassium channel KirBac1.1 in the closed state publication-title: Science – volume: 455 start-page: 497 year: 2008 end-page: 502 article-title: Crystal structure of opsin in its G‐protein‐interacting conformation publication-title: Nature – ident: emboj2009208-b43 doi: 10.1126/SCIENCE.1062023 – ident: emboj2009208-b8 doi: 10.1107/S0907444994003112 – ident: emboj2009208-b1 doi: 10.1021/bi061088h – ident: emboj2009208-b15 doi: 10.1126/science.3136547 – ident: emboj2009208-b35 doi: 10.1038/nature07330 – ident: emboj2009208-b45 doi: 10.1038/nature03018 – ident: emboj2009208-b18 doi: 10.1038/371164a0 – ident: emboj2009208-b26 doi: 10.1107/S0021889807021206 – ident: emboj2009208-b28 – ident: emboj2009208-b32 – ident: emboj2009208-b19 doi: 10.1124/mol.107.034348 – ident: emboj2009208-b23 doi: 10.1126/science.1085028 – ident: emboj2009208-b25 doi: 10.1073/pnas.242338299 – ident: emboj2009208-b38 doi: 10.1016/S0006-3495(93)81293-1 – ident: emboj2009208-b31 doi: 10.1073/pnas.0702623104 – ident: emboj2009208-b30 doi: 10.1038/nsmb1129 – ident: emboj2009208-b41 – ident: emboj2009208-b14 doi: 10.1074/jbc.M604867200 – ident: emboj2009208-b27 doi: 10.1107/S0907444996012255 – ident: emboj2009208-b4 doi: 10.1107/S0907444903017694 – ident: emboj2009208-b29 doi: 10.1038/nrm2299 – volume: 426 start-page: 419 year: 2008 ident: emboj2009208-b46 publication-title: Methods Mol Biol doi: 10.1007/978-1-60327-058-8_28 – ident: emboj2009208-b2 doi: 10.1038/nature07462 – ident: emboj2009208-b37 doi: 10.1107/S0108767307043930 – ident: emboj2009208-b6 doi: 10.1007/s10534-006-0003-2 – ident: emboj2009208-b9 doi: 10.1126/science.1109730 – volume: 11 start-page: 192 year: 2003 ident: emboj2009208-b16 publication-title: Trends Microbiol doi: 10.1016/S0966-842X(03)00100-8 – ident: emboj2009208-b44 doi: 10.1016/0092-8674(95)90220-1 – ident: emboj2009208-b10 doi: 10.1093/nar/gkm216 – ident: emboj2009208-b40 doi: 10.1146/annurev.biochem.66.1.639 – ident: emboj2009208-b5 doi: 10.1016/S0092-8674(00)81212-X – ident: emboj2009208-b7 doi: 10.1016/j.cell.2004.10.030 – ident: emboj2009208-b12 doi: 10.1016/j.jmb.2007.11.027 – volume: 26 start-page: 11 year: 1992 ident: emboj2009208-b24 publication-title: Joint CCP4+ ESF-EAMCB Newslett Protein Crystallogr – ident: emboj2009208-b13 doi: 10.1126/science.1127121 – ident: emboj2009208-b22 doi: 10.1038/nrm2438 – ident: emboj2009208-b20 doi: 10.1073/pnas.0608599104 – ident: emboj2009208-b42 doi: 10.1126/science.1118890 – ident: emboj2009208-b36 doi: 10.1038/374378a0 – ident: emboj2009208-b39 doi: 10.1073/pnas.081441398 – ident: emboj2009208-b33 doi: 10.1038/nrm2646 – ident: emboj2009208-b3 doi: 10.1038/349117a0 – ident: emboj2009208-b17 doi: 10.1016/j.sbi.2007.07.003 – ident: emboj2009208-b21 doi: 10.1107/S0108767390010224 – ident: emboj2009208-b11 doi: 10.1107/S0907444904019158 – ident: emboj2009208-b34 doi: 10.1016/j.cellsig.2008.04.012 |
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| SubjectTerms | Binding Sites Biological Transport Cation Transport Proteins - chemistry Cation Transport Proteins - metabolism crystallography Cytoplasm - metabolism EMBO37 EMBO40 Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism GDP release GTP-Binding Proteins - chemistry GTP-Binding Proteins - metabolism GTPase Guanosine Diphosphate - chemistry Guanosine Diphosphate - metabolism Iron - metabolism iron transport Membrane processes Membranes Models, Molecular Molecular biology Molecular structure Protein Conformation Proteins Signal Transduction |
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| Title | Structural basis of GDP release and gating in G protein coupled Fe2+ transport |
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