Structure of the PduU Shell Protein from the Pdu Microcompartment of Salmonella
The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica. It encapsulates several related enzymes within a shell composed of a few thousand protein subunits. Recent structural studies on the carboxysom...
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| Published in | Structure (London) Vol. 16; no. 9; pp. 1324 - 1332 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
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United States
Elsevier Inc
10.09.2008
Elsevier |
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| Online Access | Get full text |
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| Abstract | The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in
Salmonella enterica. It encapsulates several related enzymes within a shell composed of a few thousand protein subunits. Recent structural studies on the carboxysome, a related microcompartment involved in CO
2 fixation, have concluded that the major shell proteins from that microcompartment form hexamers that pack into layers comprising the facets of the shell. Here we report the crystal structure of PduU, a protein from the Pdu microcompartment, representing the first structure of a shell protein from a noncarboxysome microcompartment. Though PduU is a hexamer like other characterized shell proteins, it has undergone a circular permutation leading to dramatic differences in the hexamer pore. In view of the hypothesis that microcompartment metabolites diffuse across the outer shell through these pores, the unique structure of PduU suggests the possibility of a special functional role. |
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| AbstractList | The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica. It encapsulates several related enzymes within a shell composed of a few thousand protein subunits. Recent structural studies on the carboxysome, a related microcompartment involved in CO sub(2) fixation, have concluded that the major shell proteins from that microcompartment form hexamers that pack into layers comprising the facets of the shell. Here we report the crystal structure of PduU, a protein from the Pdu microcompartment, representing the first structure of a shell protein from a noncarboxysome microcompartment. Though PduU is a hexamer like other characterized shell proteins, it has undergone a circular permutation leading to dramatic differences in the hexamer pore. In view of the hypothesis that microcompartment metabolites diffuse across the outer shell through these pores, the unique structure of PduU suggests the possibility of a special functional role. The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica. It encapsulates several related enzymes within a shell composed of a few thousand protein subunits. Recent structural studies on the carboxysome, a related microcompartment involved in CO(2) fixation, have concluded that the major shell proteins from that microcompartment form hexamers that pack into layers comprising the facets of the shell. Here we report the crystal structure of PduU, a protein from the Pdu microcompartment, representing the first structure of a shell protein from a noncarboxysome microcompartment. Though PduU is a hexamer like other characterized shell proteins, it has undergone a circular permutation leading to dramatic differences in the hexamer pore. In view of the hypothesis that microcompartment metabolites diffuse across the outer shell through these pores, the unique structure of PduU suggests the possibility of a special functional role. The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica . It encapsulates several related enzymes within a shell composed of a few thousand protein subunits. Recent structural studies on the carboxysome, a related microcompartment involved in CO 2 fixation, have concluded that the major shell proteins from that microcompartment form hexamers that pack into layers comprising the facets of the shell. Here we report the crystal structure of PduU, a protein from the Pdu microcompartment, representing the first structure of a shell protein from a non-carboxysome microcompartment. While PduU is a hexamer like other characterized shell proteins, it has undergone a circular permutation leading to dramatic differences in the hexamer pore. In view of the hypothesis that microcompartment metabolites diffuse across the outer shell through these pores, the unique structure of PduU suggests the possibility of a special functional role. The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica. It encapsulates several related enzymes within a shell composed of a few thousand protein subunits. Recent structural studies on the carboxysome, a related microcompartment involved in CO 2 fixation, have concluded that the major shell proteins from that microcompartment form hexamers that pack into layers comprising the facets of the shell. Here we report the crystal structure of PduU, a protein from the Pdu microcompartment, representing the first structure of a shell protein from a noncarboxysome microcompartment. Though PduU is a hexamer like other characterized shell proteins, it has undergone a circular permutation leading to dramatic differences in the hexamer pore. In view of the hypothesis that microcompartment metabolites diffuse across the outer shell through these pores, the unique structure of PduU suggests the possibility of a special functional role. |
| Author | Bobik, Thomas A. Yeates, Todd O. Crowley, Christopher S. Sawaya, Michael R. |
| AuthorAffiliation | 2 UCLA-DOE Institute for Genomics and Proteomics; UCLA; Los Angeles, CA, 90095; USA 1 UCLA Molecular Biology Institute; University of California, Los Angeles (UCLA); Los Angeles, CA, 90095; USA 4 UCLA Department of Chemistry and Biochemistry; UCLA; Los Angeles, CA, 90095; USA 3 Department of Biochemistry, Biophysics and Molecular Biology; Iowa State University; Ames, IA, 50011; USA |
| AuthorAffiliation_xml | – name: 4 UCLA Department of Chemistry and Biochemistry; UCLA; Los Angeles, CA, 90095; USA – name: 1 UCLA Molecular Biology Institute; University of California, Los Angeles (UCLA); Los Angeles, CA, 90095; USA – name: 2 UCLA-DOE Institute for Genomics and Proteomics; UCLA; Los Angeles, CA, 90095; USA – name: 3 Department of Biochemistry, Biophysics and Molecular Biology; Iowa State University; Ames, IA, 50011; USA |
| Author_xml | – sequence: 1 givenname: Christopher S. surname: Crowley fullname: Crowley, Christopher S. organization: University of California Los Angeles Molecular Biology Institute, University of California Los Angeles, Los Angeles, CA 90095, USA – sequence: 2 givenname: Michael R. surname: Sawaya fullname: Sawaya, Michael R. organization: University of California Los Angeles-Department of Energy Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA – sequence: 3 givenname: Thomas A. surname: Bobik fullname: Bobik, Thomas A. organization: Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA – sequence: 4 givenname: Todd O. surname: Yeates fullname: Yeates, Todd O. email: yeates@mbi.ucla.edu organization: University of California Los Angeles Molecular Biology Institute, University of California Los Angeles, Los Angeles, CA 90095, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18786396$$D View this record in MEDLINE/PubMed https://www.osti.gov/biblio/2301812$$D View this record in Osti.gov |
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| Cites_doi | 10.1128/JB.186.23.7881-7887.2004 10.1099/mic.0.2006/004747-0 10.1006/jsbi.2001.4335 10.1126/science.1077945 10.1073/pnas.76.7.3218 10.1016/j.jmb.2006.09.024 10.1126/science.182.4112.584 10.1002/pro.5560020916 10.1107/S0907444994003112 10.1073/pnas.95.8.4641 10.1107/S0907444996012255 10.1007/s00203-003-0601-0 10.1104/pp.100.2.784 10.1128/jb.101.2.618-627.1970 10.1107/S0907444904026460 10.1128/JB.187.23.8039-8046.2005 10.1128/jb.177.5.1357-1366.1995 10.1128/JB.184.5.1253-1261.2002 10.1128/jb.176.17.5474-5482.1994 10.1128/jb.179.21.6633-6639.1997 10.1128/JB.01925-07 10.1016/S0076-6879(97)76066-X 10.1126/science.1113397 10.1016/S0026-0495(64)80018-4 10.1074/jbc.M212073200 10.1073/pnas.91.22.10417 10.1016/S0968-0004(00)89003-9 10.1093/nar/gkh340 10.1128/JB.181.19.5967-5975.1999 10.1128/JB.185.17.5086-5095.2003 10.1128/JB.181.3.799-807.1999 10.1016/j.jmb.2007.06.059 10.1007/s00253-005-0295-0 10.1371/journal.pbio.0050144 10.1128/jb.97.3.1486-1493.1969 10.1016/0022-2836(71)90324-X 10.1126/science.1151458 10.1016/S0005-2736(02)00577-1 10.1042/BST0350508 10.1007/BF00408629 10.1016/0022-2836(94)90064-7 10.1074/mcp.M600139-MCP200 10.1128/JB.183.5.1577-1584.2001 10.1128/jb.174.7.2253-2266.1992 10.1107/S0907444905001617 10.1107/S0907444904019158 |
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| References | (bib9) 1994; 50 Murzin, Lesk, Chothia (bib36) 1994; 236 Price, Coleman, Badger (bib39) 1992; 100 Shively, Decker, Greenawalt (bib43) 1970; 101 Leal, Havemann, Bobik (bib32) 2003; 180 Bobik (bib3) 2006; 70 Iancu, Ding, Morris, Dias, Gonzales, Martino, Jensen (bib24) 2007; 372 Tanaka, Kerfeld, Sawaya, Cai, Heinhorst, Cannon, Yeates (bib47) 2008; 319 Bobik, Ailion, Roth (bib4) 1992; 174 Havemann, Bobik (bib20) 2003; 185 Adkins, Mottaz, Norbeck, Gustin, Rue, Clauss, Purvine, Rodland, Heffron, Smith (bib1) 2006; 5 Tsai, Sawaya, Cannon, Cai, Williams, Heinhorst, Kerfeld, Yeates (bib48) 2007; 5 Brinsmade, Paldon, Escalante-Semerena (bib7) 2005; 187 Grishin (bib18) 2001; 134 Bobik, Havemann, Busch, Williams, Aldrich (bib6) 1999; 181 Jensen, Bowen (bib25) 1961; 68 Edgar (bib14) 2004; 32 Gantt, Conti (bib17) 1969; 97 Krissinel, Henrick (bib31) 2004; 60 Colovos, Yeates (bib10) 1993; 2 Heinhorst, Cannon, Shively (bib22) 2006 Murshudov, Vagin, Dodson (bib35) 1997; 53 Emsley, Cowtan (bib15) 2004; 60 Johnson, Pechonick, Park, Havemann, Leal, Bobik (bib26) 2001; 183 Lee, Richards (bib33) 1971; 55 Cunningham, Hemperly, Hopp, Edelman (bib12) 1979; 76 Hahn, Piotukh, Borriss, Heinemann (bib19) 1994; 91 Koprowski, Kubalski (bib30) 2003; 278 Kerfeld, Sawaya, Tanaka, Nguyen, Phillips, Beeby, Yeates (bib28) 2005; 309 Chen, Andersson, Roth (bib8) 1994; 176 Yeates, Tsai, Tanaka, Sawaya, Kerfeld (bib49) 2007; 35 Shively, Bradburne, Aldrich, Bobik, Mehlman, Jin, Baker (bib45) 1998; 76 Otwinowski, Minor (bib37) 1997; 276 Sampson, Bobik (bib40) 2008; 190 Drews, Niklowitz (bib13) 1956; 24 McCoy, Grosse-Kunstleve, Storoni, Read (bib34) 2005; 61 Bobik, Xu, Jeter, Otto, Roth (bib5) 1997; 179 Ferguson (bib16) 1964; 13 Klumpp, Fuchs (bib29) 2007; 153 Bass, Strop, Barclay, Rees (bib2) 2002; 298 Heithoff, Conner, Hentschel, Govantes, Hanna, Mahan (bib23) 1999; 181 Ponting, Russell (bib38) 1995; 20 Schulz (bib42) 2002; 1565 Conner, Heithoff, Julio, Sinsheimer, Mahan (bib11) 1998; 95 Johnson, Buszko, Bobik (bib27) 2004; 186 Stojiljkovic, Baumler, Heffron (bib46) 1995; 177 Havemann, Sampson, Bobik (bib21) 2002; 184 Schmid, Paredes, Khant, Soyer, Aldrich, Chiu, Shively (bib41) 2006; 364 Shively, Ball, Brown, Saunders (bib44) 1973; 182 Iancu (10.1016/j.str.2008.05.013_bib24) 2007; 372 Krissinel (10.1016/j.str.2008.05.013_bib31) 2004; 60 Price (10.1016/j.str.2008.05.013_bib39) 1992; 100 Heinhorst (10.1016/j.str.2008.05.013_bib22) 2006 Tsai (10.1016/j.str.2008.05.013_bib48) 2007; 5 Heithoff (10.1016/j.str.2008.05.013_bib23) 1999; 181 Johnson (10.1016/j.str.2008.05.013_bib26) 2001; 183 Brinsmade (10.1016/j.str.2008.05.013_bib7) 2005; 187 Sampson (10.1016/j.str.2008.05.013_bib40) 2008; 190 Grishin (10.1016/j.str.2008.05.013_bib18) 2001; 134 Schulz (10.1016/j.str.2008.05.013_bib42) 2002; 1565 Jensen (10.1016/j.str.2008.05.013_bib25) 1961; 68 Adkins (10.1016/j.str.2008.05.013_bib1) 2006; 5 Hahn (10.1016/j.str.2008.05.013_bib19) 1994; 91 Johnson (10.1016/j.str.2008.05.013_bib27) 2004; 186 Bass (10.1016/j.str.2008.05.013_bib2) 2002; 298 Bobik (10.1016/j.str.2008.05.013_bib5) 1997; 179 Murshudov (10.1016/j.str.2008.05.013_bib35) 1997; 53 Ferguson (10.1016/j.str.2008.05.013_bib16) 1964; 13 Kerfeld (10.1016/j.str.2008.05.013_bib28) 2005; 309 Bobik (10.1016/j.str.2008.05.013_bib6) 1999; 181 Drews (10.1016/j.str.2008.05.013_bib13) 1956; 24 Schmid (10.1016/j.str.2008.05.013_bib41) 2006; 364 Otwinowski (10.1016/j.str.2008.05.013_bib37) 1997; 276 Murzin (10.1016/j.str.2008.05.013_bib36) 1994; 236 Conner (10.1016/j.str.2008.05.013_bib11) 1998; 95 Havemann (10.1016/j.str.2008.05.013_bib20) 2003; 185 (10.1016/j.str.2008.05.013_bib9) 1994; 50 Shively (10.1016/j.str.2008.05.013_bib45) 1998; 76 Stojiljkovic (10.1016/j.str.2008.05.013_bib46) 1995; 177 Colovos (10.1016/j.str.2008.05.013_bib10) 1993; 2 Edgar (10.1016/j.str.2008.05.013_bib14) 2004; 32 Shively (10.1016/j.str.2008.05.013_bib44) 1973; 182 Cunningham (10.1016/j.str.2008.05.013_bib12) 1979; 76 Klumpp (10.1016/j.str.2008.05.013_bib29) 2007; 153 Leal (10.1016/j.str.2008.05.013_bib32) 2003; 180 Bobik (10.1016/j.str.2008.05.013_bib4) 1992; 174 Ponting (10.1016/j.str.2008.05.013_bib38) 1995; 20 Shively (10.1016/j.str.2008.05.013_bib43) 1970; 101 Yeates (10.1016/j.str.2008.05.013_bib49) 2007; 35 Bobik (10.1016/j.str.2008.05.013_bib3) 2006; 70 Emsley (10.1016/j.str.2008.05.013_bib15) 2004; 60 McCoy (10.1016/j.str.2008.05.013_bib34) 2005; 61 Chen (10.1016/j.str.2008.05.013_bib8) 1994; 176 Lee (10.1016/j.str.2008.05.013_bib33) 1971; 55 Koprowski (10.1016/j.str.2008.05.013_bib30) 2003; 278 Tanaka (10.1016/j.str.2008.05.013_bib47) 2008; 319 Gantt (10.1016/j.str.2008.05.013_bib17) 1969; 97 Havemann (10.1016/j.str.2008.05.013_bib21) 2002; 184 |
| References_xml | – volume: 134 start-page: 167 year: 2001 end-page: 185 ident: bib18 article-title: Fold change in evolution of protein structures publication-title: J. Struct. Biol. contributor: fullname: Grishin – volume: 185 start-page: 5086 year: 2003 end-page: 5095 ident: bib20 article-title: Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in publication-title: J. Bacteriol. contributor: fullname: Bobik – volume: 187 start-page: 8039 year: 2005 end-page: 8046 ident: bib7 article-title: Minimal functions and physiological conditions required for growth of publication-title: J. Bacteriol. contributor: fullname: Escalante-Semerena – volume: 76 start-page: 906 year: 1998 end-page: 916 ident: bib45 article-title: Sequence homologs of the carboxysomal polypeptide CsoS1 of the thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes-polyhedral bodies publication-title: Can. J. Bot. contributor: fullname: Baker – volume: 278 start-page: 11237 year: 2003 end-page: 11245 ident: bib30 article-title: C termini of the Escherichia coli mechanosensitive ion channel (MscS) move apart upon the channel opening publication-title: J. Biol. Chem. contributor: fullname: Kubalski – volume: 101 start-page: 618 year: 1970 end-page: 627 ident: bib43 article-title: Comparative ultrastructure of the publication-title: J. Bacteriol. contributor: fullname: Greenawalt – volume: 20 start-page: 179 year: 1995 end-page: 180 ident: bib38 article-title: Swaposins: circular permutations within genes encoding saposin homologues publication-title: Trends Biochem. Sci. contributor: fullname: Russell – volume: 68 start-page: 86 year: 1961 end-page: 89 ident: bib25 article-title: Organization of the centroplasm in Nostoc pruniforme publication-title: Iowa Acad. Sci. Proc. contributor: fullname: Bowen – volume: 177 start-page: 1357 year: 1995 end-page: 1366 ident: bib46 article-title: Ethanolamine utilization in publication-title: J. Bacteriol. contributor: fullname: Heffron – volume: 53 start-page: 240 year: 1997 end-page: 255 ident: bib35 article-title: Refinement of macromolecular structures by the maximum-likelihood method publication-title: Acta Crystallogr. D Biol. Crystallogr. contributor: fullname: Dodson – start-page: 141 year: 2006 end-page: 165 ident: bib22 article-title: Carboxysomes and carboxysome-like inclusions publication-title: Complex Intracellular Structures in Prokaryotes contributor: fullname: Shively – volume: 55 start-page: 379 year: 1971 end-page: 400 ident: bib33 article-title: The interpretation of protein structures: estimation of static accessibility publication-title: J. Mol. Biol. contributor: fullname: Richards – volume: 13 start-page: 985 year: 1964 end-page: 1002 ident: bib16 article-title: Starch-gel electrophoresis—application to the classification of pituitary proteins and polypeptides publication-title: Metabolism contributor: fullname: Ferguson – volume: 184 start-page: 1253 year: 2002 end-page: 1261 ident: bib21 article-title: PduA is a shell protein of polyhedral organelles involved in coenzyme B(12)-dependent degradation of 1,2-propanediol in publication-title: J. Bacteriol. contributor: fullname: Bobik – volume: 319 start-page: 1083 year: 2008 end-page: 1086 ident: bib47 article-title: Atomic-level models of the bacterial carboxysome shell publication-title: Science contributor: fullname: Yeates – volume: 180 start-page: 353 year: 2003 end-page: 361 ident: bib32 article-title: PduP is a coenzyme-a-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B12-dependent 1,2-propanediol degradation by publication-title: Arch. Microbiol. contributor: fullname: Bobik – volume: 97 start-page: 1486 year: 1969 end-page: 1493 ident: bib17 article-title: Ultrastructure of blue-green algae publication-title: J. Bacteriol. contributor: fullname: Conti – volume: 183 start-page: 1577 year: 2001 end-page: 1584 ident: bib26 article-title: Functional genomic, biochemical, and genetic characterization of the publication-title: J. Bacteriol. contributor: fullname: Bobik – volume: 309 start-page: 936 year: 2005 end-page: 938 ident: bib28 article-title: Protein structures forming the shell of primitive bacterial organelles publication-title: Science contributor: fullname: Yeates – volume: 276 start-page: 307 year: 1997 end-page: 326 ident: bib37 article-title: Processing of X-ray diffraction data collected in oscillation mode publication-title: Methods Enzymol. contributor: fullname: Minor – volume: 2 start-page: 1511 year: 1993 end-page: 1519 ident: bib10 article-title: Verification of protein structures: patterns of nonbonded atomic interactions publication-title: Protein Sci. contributor: fullname: Yeates – volume: 24 start-page: 147 year: 1956 end-page: 162 ident: bib13 article-title: Cytology of cyanophycea. II. Centroplasm and granular inclusions of Phormidium uncinatum publication-title: Arch. Mikrobiol. contributor: fullname: Niklowitz – volume: 91 start-page: 10417 year: 1994 end-page: 10421 ident: bib19 article-title: Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis publication-title: Proc. Natl. Acad. Sci. U.S.A. contributor: fullname: Heinemann – volume: 186 start-page: 7881 year: 2004 end-page: 7887 ident: bib27 article-title: Purification and initial characterization of the publication-title: J. Bacteriol. contributor: fullname: Bobik – volume: 76 start-page: 3218 year: 1979 end-page: 3222 ident: bib12 article-title: Favin versus concanavalin A: circularly permuted amino acid sequences publication-title: Proc. Natl. Acad. Sci. U.S.A. contributor: fullname: Edelman – volume: 181 start-page: 799 year: 1999 end-page: 807 ident: bib23 article-title: Coordinate intracellular expression of publication-title: J. Bacteriol. contributor: fullname: Mahan – volume: 5 start-page: 1450 year: 2006 end-page: 1461 ident: bib1 article-title: Analysis of the publication-title: Mol. Cell. Proteomics contributor: fullname: Smith – volume: 182 start-page: 584 year: 1973 end-page: 586 ident: bib44 article-title: Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus publication-title: Science contributor: fullname: Saunders – volume: 5 start-page: e144 year: 2007 ident: bib48 article-title: Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome publication-title: PLoS Biol. contributor: fullname: Yeates – volume: 32 start-page: 1792 year: 2004 end-page: 1797 ident: bib14 article-title: MUSCLE: multiple sequence alignment with high accuracy and high throughput publication-title: Nucleic Acids Res. contributor: fullname: Edgar – volume: 153 start-page: 1207 year: 2007 end-page: 1220 ident: bib29 article-title: Identification of novel genes in genomic islands that contribute to publication-title: Microbiology contributor: fullname: Fuchs – volume: 1565 start-page: 308 year: 2002 end-page: 317 ident: bib42 article-title: The structure of bacterial outer membrane proteins publication-title: Biochim. Biophys. Acta contributor: fullname: Schulz – volume: 70 start-page: 517 year: 2006 end-page: 525 ident: bib3 article-title: Polyhedral organelles compartmenting bacterial metabolic processes publication-title: Appl. Microbiol. Biotechnol. contributor: fullname: Bobik – volume: 60 start-page: 2126 year: 2004 end-page: 2132 ident: bib15 article-title: Coot: model-building tools for molecular graphics publication-title: Acta Crystallogr. D Biol. Crystallogr. contributor: fullname: Cowtan – volume: 100 start-page: 784 year: 1992 end-page: 793 ident: bib39 article-title: Association of carbonic anhydrase activity with carboxysomes isolated from the cyanobacterium publication-title: Plant Physiol. contributor: fullname: Badger – volume: 372 start-page: 764 year: 2007 end-page: 773 ident: bib24 article-title: The structure of isolated synechococcus strain WH8102 carboxysomes as revealed by electron cryotomography publication-title: J. Mol. Biol. contributor: fullname: Jensen – volume: 174 start-page: 2253 year: 1992 end-page: 2266 ident: bib4 article-title: A single regulatory gene integrates control of vitamin B12 synthesis and propanediol degradation publication-title: J. Bacteriol. contributor: fullname: Roth – volume: 181 start-page: 5967 year: 1999 end-page: 5975 ident: bib6 article-title: The propanediol utilization ( publication-title: J. Bacteriol. contributor: fullname: Aldrich – volume: 50 start-page: 760 year: 1994 end-page: 763 ident: bib9 article-title: The CCP4 suite: programs for protein crystallography publication-title: Acta Crystallogr. D Biol. Crystallogr. – volume: 61 start-page: 458 year: 2005 end-page: 464 ident: bib34 article-title: Likelihood-enhanced fast translation functions publication-title: Acta Crystallogr. D Biol. Crystallogr. contributor: fullname: Read – volume: 176 start-page: 5474 year: 1994 end-page: 5482 ident: bib8 article-title: The control region of the publication-title: J. Bacteriol. contributor: fullname: Roth – volume: 298 start-page: 1582 year: 2002 end-page: 1587 ident: bib2 article-title: Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel publication-title: Science contributor: fullname: Rees – volume: 35 start-page: 508 year: 2007 end-page: 511 ident: bib49 article-title: Self-assembly in the carboxysome: a viral capsid-like protein shell in bacterial cells publication-title: Biochem. Soc. Trans. contributor: fullname: Kerfeld – volume: 95 start-page: 4641 year: 1998 end-page: 4645 ident: bib11 article-title: Differential patterns of acquired virulence genes distinguish publication-title: Proc. Natl. Acad. Sci. U.S.A. contributor: fullname: Mahan – volume: 60 start-page: 2256 year: 2004 end-page: 2268 ident: bib31 article-title: Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions publication-title: Acta Crystallogr. D Biol. Crystallogr. contributor: fullname: Henrick – volume: 236 start-page: 1369 year: 1994 end-page: 1381 ident: bib36 article-title: Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis publication-title: J. Mol. Biol. contributor: fullname: Chothia – volume: 179 start-page: 6633 year: 1997 end-page: 6639 ident: bib5 article-title: Propanediol utilization genes ( publication-title: J. Bacteriol. contributor: fullname: Roth – volume: 364 start-page: 526 year: 2006 end-page: 535 ident: bib41 article-title: Structure of Halothiobacillus neapolitanus carboxysomes by cryo-electron tomography publication-title: J. Mol. Biol. contributor: fullname: Shively – volume: 190 start-page: 2966 year: 2008 end-page: 2971 ident: bib40 article-title: Microcompartments for B12-dependent 1,2-propanediol degradation provide protection from DNA and cellular damage by a reactive metabolic intermediate publication-title: J. Bacteriol. contributor: fullname: Bobik – volume: 186 start-page: 7881 year: 2004 ident: 10.1016/j.str.2008.05.013_bib27 article-title: Purification and initial characterization of the Salmonella enterica PduO ATP:Cob(I)alamin adenosyltransferase publication-title: J. Bacteriol. doi: 10.1128/JB.186.23.7881-7887.2004 contributor: fullname: Johnson – volume: 153 start-page: 1207 year: 2007 ident: 10.1016/j.str.2008.05.013_bib29 article-title: Identification of novel genes in genomic islands that contribute to Salmonella typhimurium replication in macrophages publication-title: Microbiology doi: 10.1099/mic.0.2006/004747-0 contributor: fullname: Klumpp – volume: 134 start-page: 167 year: 2001 ident: 10.1016/j.str.2008.05.013_bib18 article-title: Fold change in evolution of protein structures publication-title: J. Struct. Biol. doi: 10.1006/jsbi.2001.4335 contributor: fullname: Grishin – volume: 298 start-page: 1582 year: 2002 ident: 10.1016/j.str.2008.05.013_bib2 article-title: Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel publication-title: Science doi: 10.1126/science.1077945 contributor: fullname: Bass – volume: 76 start-page: 3218 year: 1979 ident: 10.1016/j.str.2008.05.013_bib12 article-title: Favin versus concanavalin A: circularly permuted amino acid sequences publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.76.7.3218 contributor: fullname: Cunningham – volume: 364 start-page: 526 year: 2006 ident: 10.1016/j.str.2008.05.013_bib41 article-title: Structure of Halothiobacillus neapolitanus carboxysomes by cryo-electron tomography publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2006.09.024 contributor: fullname: Schmid – volume: 182 start-page: 584 year: 1973 ident: 10.1016/j.str.2008.05.013_bib44 article-title: Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus publication-title: Science doi: 10.1126/science.182.4112.584 contributor: fullname: Shively – volume: 2 start-page: 1511 year: 1993 ident: 10.1016/j.str.2008.05.013_bib10 article-title: Verification of protein structures: patterns of nonbonded atomic interactions publication-title: Protein Sci. doi: 10.1002/pro.5560020916 contributor: fullname: Colovos – volume: 50 start-page: 760 year: 1994 ident: 10.1016/j.str.2008.05.013_bib9 article-title: The CCP4 suite: programs for protein crystallography publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444994003112 – volume: 95 start-page: 4641 year: 1998 ident: 10.1016/j.str.2008.05.013_bib11 article-title: Differential patterns of acquired virulence genes distinguish Salmonella strains publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.95.8.4641 contributor: fullname: Conner – volume: 53 start-page: 240 year: 1997 ident: 10.1016/j.str.2008.05.013_bib35 article-title: Refinement of macromolecular structures by the maximum-likelihood method publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444996012255 contributor: fullname: Murshudov – volume: 180 start-page: 353 year: 2003 ident: 10.1016/j.str.2008.05.013_bib32 article-title: PduP is a coenzyme-a-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2 publication-title: Arch. Microbiol. doi: 10.1007/s00203-003-0601-0 contributor: fullname: Leal – volume: 100 start-page: 784 year: 1992 ident: 10.1016/j.str.2008.05.013_bib39 article-title: Association of carbonic anhydrase activity with carboxysomes isolated from the cyanobacterium Synechococcus PCC7942 publication-title: Plant Physiol. doi: 10.1104/pp.100.2.784 contributor: fullname: Price – volume: 101 start-page: 618 year: 1970 ident: 10.1016/j.str.2008.05.013_bib43 article-title: Comparative ultrastructure of the Thiobacilli publication-title: J. Bacteriol. doi: 10.1128/jb.101.2.618-627.1970 contributor: fullname: Shively – volume: 60 start-page: 2256 year: 2004 ident: 10.1016/j.str.2008.05.013_bib31 article-title: Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444904026460 contributor: fullname: Krissinel – volume: 187 start-page: 8039 year: 2005 ident: 10.1016/j.str.2008.05.013_bib7 article-title: Minimal functions and physiological conditions required for growth of Salmonella enterica on ethanolamine in the absence of the metabolosome publication-title: J. Bacteriol. doi: 10.1128/JB.187.23.8039-8046.2005 contributor: fullname: Brinsmade – volume: 177 start-page: 1357 year: 1995 ident: 10.1016/j.str.2008.05.013_bib46 article-title: Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster publication-title: J. Bacteriol. doi: 10.1128/jb.177.5.1357-1366.1995 contributor: fullname: Stojiljkovic – volume: 68 start-page: 86 year: 1961 ident: 10.1016/j.str.2008.05.013_bib25 article-title: Organization of the centroplasm in Nostoc pruniforme publication-title: Iowa Acad. Sci. Proc. contributor: fullname: Jensen – volume: 184 start-page: 1253 year: 2002 ident: 10.1016/j.str.2008.05.013_bib21 article-title: PduA is a shell protein of polyhedral organelles involved in coenzyme B(12)-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2 publication-title: J. Bacteriol. doi: 10.1128/JB.184.5.1253-1261.2002 contributor: fullname: Havemann – volume: 176 start-page: 5474 year: 1994 ident: 10.1016/j.str.2008.05.013_bib8 article-title: The control region of the pdu/cob regulon in Salmonella typhimurium publication-title: J. Bacteriol. doi: 10.1128/jb.176.17.5474-5482.1994 contributor: fullname: Chen – volume: 179 start-page: 6633 year: 1997 ident: 10.1016/j.str.2008.05.013_bib5 article-title: Propanediol utilization genes (pdu) of Salmonella typhimurium: three genes for the propanediol dehydratase publication-title: J. Bacteriol. doi: 10.1128/jb.179.21.6633-6639.1997 contributor: fullname: Bobik – volume: 190 start-page: 2966 year: 2008 ident: 10.1016/j.str.2008.05.013_bib40 article-title: Microcompartments for B12-dependent 1,2-propanediol degradation provide protection from DNA and cellular damage by a reactive metabolic intermediate publication-title: J. Bacteriol. doi: 10.1128/JB.01925-07 contributor: fullname: Sampson – volume: 276 start-page: 307 year: 1997 ident: 10.1016/j.str.2008.05.013_bib37 article-title: Processing of X-ray diffraction data collected in oscillation mode publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(97)76066-X contributor: fullname: Otwinowski – volume: 309 start-page: 936 year: 2005 ident: 10.1016/j.str.2008.05.013_bib28 article-title: Protein structures forming the shell of primitive bacterial organelles publication-title: Science doi: 10.1126/science.1113397 contributor: fullname: Kerfeld – volume: 13 start-page: 985 issue: Suppl year: 1964 ident: 10.1016/j.str.2008.05.013_bib16 article-title: Starch-gel electrophoresis—application to the classification of pituitary proteins and polypeptides publication-title: Metabolism doi: 10.1016/S0026-0495(64)80018-4 contributor: fullname: Ferguson – volume: 278 start-page: 11237 year: 2003 ident: 10.1016/j.str.2008.05.013_bib30 article-title: C termini of the Escherichia coli mechanosensitive ion channel (MscS) move apart upon the channel opening publication-title: J. Biol. Chem. doi: 10.1074/jbc.M212073200 contributor: fullname: Koprowski – volume: 91 start-page: 10417 year: 1994 ident: 10.1016/j.str.2008.05.013_bib19 article-title: Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.91.22.10417 contributor: fullname: Hahn – volume: 20 start-page: 179 year: 1995 ident: 10.1016/j.str.2008.05.013_bib38 article-title: Swaposins: circular permutations within genes encoding saposin homologues publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(00)89003-9 contributor: fullname: Ponting – volume: 32 start-page: 1792 year: 2004 ident: 10.1016/j.str.2008.05.013_bib14 article-title: MUSCLE: multiple sequence alignment with high accuracy and high throughput publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh340 contributor: fullname: Edgar – volume: 181 start-page: 5967 year: 1999 ident: 10.1016/j.str.2008.05.013_bib6 article-title: The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B(12)-dependent 1, 2-propanediol degradation publication-title: J. Bacteriol. doi: 10.1128/JB.181.19.5967-5975.1999 contributor: fullname: Bobik – volume: 185 start-page: 5086 year: 2003 ident: 10.1016/j.str.2008.05.013_bib20 article-title: Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2 publication-title: J. Bacteriol. doi: 10.1128/JB.185.17.5086-5095.2003 contributor: fullname: Havemann – start-page: 141 year: 2006 ident: 10.1016/j.str.2008.05.013_bib22 article-title: Carboxysomes and carboxysome-like inclusions contributor: fullname: Heinhorst – volume: 181 start-page: 799 year: 1999 ident: 10.1016/j.str.2008.05.013_bib23 article-title: Coordinate intracellular expression of Salmonella genes induced during infection publication-title: J. Bacteriol. doi: 10.1128/JB.181.3.799-807.1999 contributor: fullname: Heithoff – volume: 372 start-page: 764 year: 2007 ident: 10.1016/j.str.2008.05.013_bib24 article-title: The structure of isolated synechococcus strain WH8102 carboxysomes as revealed by electron cryotomography publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.06.059 contributor: fullname: Iancu – volume: 70 start-page: 517 year: 2006 ident: 10.1016/j.str.2008.05.013_bib3 article-title: Polyhedral organelles compartmenting bacterial metabolic processes publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-005-0295-0 contributor: fullname: Bobik – volume: 5 start-page: e144 year: 2007 ident: 10.1016/j.str.2008.05.013_bib48 article-title: Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome publication-title: PLoS Biol. doi: 10.1371/journal.pbio.0050144 contributor: fullname: Tsai – volume: 97 start-page: 1486 year: 1969 ident: 10.1016/j.str.2008.05.013_bib17 article-title: Ultrastructure of blue-green algae publication-title: J. Bacteriol. doi: 10.1128/jb.97.3.1486-1493.1969 contributor: fullname: Gantt – volume: 55 start-page: 379 year: 1971 ident: 10.1016/j.str.2008.05.013_bib33 article-title: The interpretation of protein structures: estimation of static accessibility publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(71)90324-X contributor: fullname: Lee – volume: 319 start-page: 1083 year: 2008 ident: 10.1016/j.str.2008.05.013_bib47 article-title: Atomic-level models of the bacterial carboxysome shell publication-title: Science doi: 10.1126/science.1151458 contributor: fullname: Tanaka – volume: 1565 start-page: 308 year: 2002 ident: 10.1016/j.str.2008.05.013_bib42 article-title: The structure of bacterial outer membrane proteins publication-title: Biochim. Biophys. Acta doi: 10.1016/S0005-2736(02)00577-1 contributor: fullname: Schulz – volume: 35 start-page: 508 year: 2007 ident: 10.1016/j.str.2008.05.013_bib49 article-title: Self-assembly in the carboxysome: a viral capsid-like protein shell in bacterial cells publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0350508 contributor: fullname: Yeates – volume: 24 start-page: 147 year: 1956 ident: 10.1016/j.str.2008.05.013_bib13 article-title: Cytology of cyanophycea. II. Centroplasm and granular inclusions of Phormidium uncinatum publication-title: Arch. Mikrobiol. doi: 10.1007/BF00408629 contributor: fullname: Drews – volume: 236 start-page: 1369 year: 1994 ident: 10.1016/j.str.2008.05.013_bib36 article-title: Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(94)90064-7 contributor: fullname: Murzin – volume: 5 start-page: 1450 year: 2006 ident: 10.1016/j.str.2008.05.013_bib1 article-title: Analysis of the Salmonella typhimurium proteome through environmental response toward infectious conditions publication-title: Mol. Cell. Proteomics doi: 10.1074/mcp.M600139-MCP200 contributor: fullname: Adkins – volume: 183 start-page: 1577 year: 2001 ident: 10.1016/j.str.2008.05.013_bib26 article-title: Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene publication-title: J. Bacteriol. doi: 10.1128/JB.183.5.1577-1584.2001 contributor: fullname: Johnson – volume: 76 start-page: 906 year: 1998 ident: 10.1016/j.str.2008.05.013_bib45 article-title: Sequence homologs of the carboxysomal polypeptide CsoS1 of the thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes-polyhedral bodies publication-title: Can. J. Bot. contributor: fullname: Shively – volume: 174 start-page: 2253 year: 1992 ident: 10.1016/j.str.2008.05.013_bib4 article-title: A single regulatory gene integrates control of vitamin B12 synthesis and propanediol degradation publication-title: J. Bacteriol. doi: 10.1128/jb.174.7.2253-2266.1992 contributor: fullname: Bobik – volume: 61 start-page: 458 year: 2005 ident: 10.1016/j.str.2008.05.013_bib34 article-title: Likelihood-enhanced fast translation functions publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444905001617 contributor: fullname: McCoy – volume: 60 start-page: 2126 year: 2004 ident: 10.1016/j.str.2008.05.013_bib15 article-title: Coot: model-building tools for molecular graphics publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444904019158 contributor: fullname: Emsley |
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| Snippet | The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in
Salmonella enterica. It... The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica. It... The Pdu microcompartment is a proteinaceous, subcellular structure that serves as an organelle for the metabolism of 1,2-propanediol in Salmonella enterica .... |
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| SubjectTerms | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacterial Proteins - physiology Cell Compartmentation - physiology Cell Wall - chemistry Cell Wall - ultrastructure Crystallography, X-Ray MICROBIO Models, Biological Models, Molecular Molecular Sequence Data Porins - chemistry Porins - metabolism Porins - physiology Protein Folding Protein Structure, Quaternary Salmonella enterica Salmonella enterica - chemistry Salmonella enterica - metabolism Salmonella enterica - ultrastructure Sequence Homology, Amino Acid |
| Title | Structure of the PduU Shell Protein from the Pdu Microcompartment of Salmonella |
| URI | https://dx.doi.org/10.1016/j.str.2008.05.013 https://www.ncbi.nlm.nih.gov/pubmed/18786396 https://search.proquest.com/docview/19568178 https://search.proquest.com/docview/69540239 https://www.osti.gov/biblio/2301812 https://pubmed.ncbi.nlm.nih.gov/PMC5878062 |
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