NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B

The fungal protein CBP ( calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology...

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Published in	Molecular microbiology Vol. 72; no. 2; pp. 344 - 353
Main Authors	Beck, Moriah R, DeKoster, Gregory T, Cistola, David P, Goldman, William E
Format	Journal Article
Language	English
Published	Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.04.2009 Blackwell Publishing Ltd Blackwell
Subjects	Amino Acid Sequence Bacterial proteins Binding sites Biological and medical sciences Calcium-Binding Proteins - chemistry Dimerization Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungi Histoplasma - chemistry Histoplasma capsulatum Lipids Microbiology Models, Molecular Molecular Sequence Data NMR Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Conformation Saposins - chemistry Virology Virulence Factors - chemistry Vertebrata Mammalia Microbiology Virulence Glycoprotein Homology NMR spectrometry
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Abstract	The fungal protein CBP ( calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four α-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells.
AbstractList	Summary The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four α‐helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells. The fungal protein CBP ( c alcium b inding p rotein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum ’s most abundant secreted protein. However, CBP has no sequence homology with other calcium binding proteins and contains no known calcium-binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four α-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid-binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells. The fungal protein CBP ( calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four α-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells. The fungal protein CBP ( c alcium b inding p rotein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum 's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four α‐helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells. The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four α-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells. [PUBLICATION ABSTRACT] SummaryThe fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four a-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells. The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four alpha-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells.
Author	Beck, Moriah R Cistola, David P Goldman, William E DeKoster, Gregory T
AuthorAffiliation	3 Department of Microbiology and Immunology, University of North Carolina at Chapel Hill 4 Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill 1 Department of Molecular Microbiology, Washington University in St. Louis 2 Department of Biochemistry and Molecular Biophysics, Washington University in St. Louis
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Cites_doi	10.1107/S0907444998003254 10.1016/S0022-2275(20)41485-3 10.1074/jbc.M101075200 10.1073/pnas.210301097 10.1016/j.abb.2005.09.007 10.1016/j.str.2008.02.016 10.1006/jmbi.1997.1044 10.1016/S0014-5793(99)01520-3 10.1006/jmbi.1993.1489 10.1016/S0076-6879(01)39310-2 10.1093/glycob/11.6.81R 10.1093/bioinformatics/btl589 10.1515/BC.1999.124 10.1084/jem.177.6.1605 10.1021/bi0301338 10.1073/pnas.0136947100 10.1126/science.290.5495.1368 10.1016/0263-7855(96)00009-4 10.1110/ps.062256606 10.1074/jbc.M312978200 10.1046/j.1462-5822.2000.00078.x 10.1023/A:1008392405740 10.1093/nar/gkh430 10.1021/bi00003a021 10.1110/ps.03602304 10.1006/jmbi.1994.0053 10.1093/emboj/18.14.3947 10.1016/S1359-0278(97)00064-3 10.1128/IAI.65.12.5257-5261.1997 10.1016/j.jmb.2003.09.060 10.1046/j.1365-2958.1998.00697.x 10.1021/ja970224q 10.1002/pro.5560050210 10.1146/annurev.cellbio.21.122303.120013 10.1021/bi701495v 10.1038/nsb1097-793 10.1021/ja00070a024 10.1002/jlb.43.6.483 10.1016/S0022-2836(03)00238-9 10.1016/S0022-2836(02)01234-2 10.1016/S0021-9258(17)46658-0 10.1107/S0021889892009944 10.1007/BF00175245 10.1021/ja026939x 10.1021/bi00449a003 10.1016/j.jmb.2006.08.009 10.1042/BJ20050051 10.1016/0958-1669(93)90002-E 10.1016/S0076-6879(94)39014-2 10.1074/jbc.M102736200
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References	1993; 26 1997; 119 1995; 36 1995; 34 2005; 21 2000; 2 1997; 2 1997; 4 1993; 4 2000; 290 1997; 269 2003; 327 2003; 325 1994b; 239 1999; 18 2005; 389 1999; 380 2002; 2007 2000; 97 1999; 13 1988; 43 2006; 362 1995; 245 2001; 339 2001; 11 1996; 5 2003; 125 2004b; 32 1998; 54 2007; 23 2003; 42 1993; 177 1998; 27 1997; 65 2008; 16 2006; 15 1999; 462 1996; 14 1993; 268 2003; 334 1989; 28 2001; 276 2004; 279 2004a; 13 2005; 443 2008; 47 1993; 115 1994a; 4 2003; 100 1993; 233 8377180 - J Mol Biol. 1993 Sep 5;233(1):123-38 15215455 - Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W582-5 18361504 - Biochemistry. 2008 Apr 15;47(15):4427-38 14623193 - J Mol Biol. 2003 Nov 28;334(3):541-9 10494853 - Biol Chem. 1999 Jul-Aug;380(7-8):1001-7 9199409 - J Mol Biol. 1997 Jun 13;269(3):408-22 8744573 - J Mol Graph. 1996 Feb;14(1):51-5, 29-32 11462826 - Methods Enzymol. 2001;339:71-90 9757107 - Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21 15215527 - Protein Sci. 2004 Jul;13(7):1841-50 9393824 - Infect Immun. 1997 Dec;65(12):5257-61 8019132 - J Biomol NMR. 1994 Mar;4(2):171-80 14674747 - Biochemistry. 2003 Dec 23;42(50):14729-40 9269569 - Fold Des. 1997;2(4):S53-7 16823039 - Protein Sci. 2006 Aug;15(8):1849-57 10406799 - EMBO J. 1999 Jul 15;18(14):3947-55 10212987 - J Biomol NMR. 1999 Mar;13(3):289-302 8745404 - Protein Sci. 1996 Feb;5(2):262-9 2454277 - J Leukoc Biol. 1988 Jun;43(6):483-91 7844833 - J Mol Biol. 1995 Feb 3;245(5):645-60 11207606 - Cell Microbiol. 2000 Dec;2(6):537-47 7830591 - Methods Enzymol. 1994;239:363-92 16949605 - J Mol Biol. 2006 Oct 6;362(5):943-53 12580598 - J Am Chem Soc. 2003 Feb 19;125(7):1731-7 16256068 - Arch Biochem Biophys. 2005 Nov 15;443(1-2):101-12 12488100 - J Mol Biol. 2003 Jan 10;325(2):355-65 12662935 - J Mol Biol. 2003 Apr 11;327(5):1121-33 8496679 - J Exp Med. 1993 Jun 1;177(6):1605-11 15992358 - Biochem J. 2005 Jul 15;389(Pt 2):249-57 12518053 - Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):38-43 11445546 - Glycobiology. 2001 Jun;11(6):81R-90R 11005847 - Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11221-6 18462685 - Structure. 2008 May;16(5):809-17 16212488 - Annu Rev Cell Dev Biol. 2005;21:81-103 7827045 - Biochemistry. 1995 Jan 24;34(3):868-78 11082066 - Science. 2000 Nov 17;290(5495):1368-72 8360153 - J Biol Chem. 1993 Sep 5;268(25):18519-23 17121777 - Bioinformatics. 2007 Feb 1;23(3):381-2 7763967 - Curr Opin Biotechnol. 1993 Aug;4(4):385-91 11406625 - J Biol Chem. 2001 Aug 24;276(34):31583-9 10580110 - FEBS Lett. 1999 Nov 26;462(1-2):155-8 2690953 - Biochemistry. 1989 Nov 14;28(23):8972-9 14970207 - J Biol Chem. 2004 Apr 23;279(17):17834-41 11356836 - J Biol Chem. 2001 Jul 20;276(29):27010-7 9334742 - Nat Struct Biol. 1997 Oct;4(10):793-5 9489665 - Mol Microbiol. 1998 Feb;27(3):531-9 7595087 - J Lipid Res. 1995 Aug;36(8):1653-63 e_1_2_6_51_1 e_1_2_6_32_1 e_1_2_6_30_1 e_1_2_6_19_1 e_1_2_6_13_1 e_1_2_6_36_1 e_1_2_6_11_1 e_1_2_6_34_1 e_1_2_6_17_1 e_1_2_6_15_1 e_1_2_6_38_1 e_1_2_6_43_1 e_1_2_6_20_1 e_1_2_6_41_1 Soeda S. (e_1_2_6_47_1) 1993; 268 e_1_2_6_9_1 e_1_2_6_5_1 e_1_2_6_7_1 e_1_2_6_24_1 e_1_2_6_49_1 e_1_2_6_3_1 e_1_2_6_22_1 e_1_2_6_28_1 e_1_2_6_45_1 e_1_2_6_26_1 e_1_2_6_52_1 e_1_2_6_10_1 e_1_2_6_31_1 e_1_2_6_50_1 DeLano W.L. (e_1_2_6_16_1) 2002 e_1_2_6_14_1 e_1_2_6_35_1 e_1_2_6_12_1 e_1_2_6_33_1 e_1_2_6_18_1 e_1_2_6_39_1 e_1_2_6_37_1 e_1_2_6_42_1 e_1_2_6_21_1 e_1_2_6_40_1 e_1_2_6_8_1 e_1_2_6_4_1 e_1_2_6_6_1 e_1_2_6_25_1 e_1_2_6_48_1 e_1_2_6_23_1 e_1_2_6_2_1 e_1_2_6_29_1 e_1_2_6_44_1 e_1_2_6_27_1 e_1_2_6_46_1
References_xml	– volume: 290 start-page: 1368 year: 2000 end-page: 1372 article-title: Intracellular parasitism by : fungal virulence and calcium dependence publication-title: Science – volume: 269 start-page: 408 year: 1997 end-page: 422 article-title: Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta‐spectrin publication-title: J Mol Biol – volume: 13 start-page: 1841 year: 2004a end-page: 1850 article-title: Database searching by flexible protein structure alignment publication-title: Protein Sci – volume: 100 start-page: 38 year: 2003 end-page: 43 article-title: Crystal structure of saposin B reveals a dimeric shell for lipid binding publication-title: Proc Natl Acad Sci USA – volume: 36 start-page: 1653 year: 1995 end-page: 1663 article-title: Saposin‐like proteins (SAPLIP) carry out diverse functions on a common backbone structure publication-title: J Lipid Res – volume: 2 start-page: 537 year: 2000 end-page: 547 article-title: Monitoring phase‐specific gene expression in with telomeric GFP fusion plasmids publication-title: Cell Microbiol – volume: 119 start-page: 6711 year: 1997 end-page: 6721 article-title: Methods for measurement of intermolecular NOEs by mulitnuclear NMR spectroscopy: application to a bacteriophage N‐peptide/boxB RNA complex publication-title: J Am Chem Soc – volume: 21 start-page: 81 year: 2005 end-page: 103 article-title: Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids publication-title: Annu Rev Cell Dev Biol – volume: 5 start-page: 262 year: 1996 end-page: 269 article-title: Yeast heat shock transcription factor N‐terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy publication-title: Protein Sci – volume: 2007 year: 2002 – volume: 279 start-page: 17834 year: 2004 end-page: 17841 article-title: Solution structure of the pore‐forming protein of publication-title: J Biol Chem – volume: 4 start-page: 385 year: 1993 end-page: 391 article-title: Dynamic properties of proteins from NMR spectroscopy publication-title: Curr Opin Biotechnol – volume: 15 start-page: 1849 year: 2006 end-page: 1857 article-title: Crystal structures of saposins A and C publication-title: Protein Sci – volume: 4 start-page: 171 year: 1994a end-page: 180 article-title: The 13C chemical‐shift index: a simple method for the identification of protein secondary structure using 13C chemical‐shift data publication-title: J Biomol NMR – volume: 125 start-page: 1731 year: 2003 end-page: 1737 article-title: HADDOCK: a protein‐protein docking approach based on biochemical or biophysical information publication-title: J Am Chem Soc – volume: 325 start-page: 355 year: 2003 end-page: 365 article-title: Granulysin crystal structure and a structure‐derived lytic mechanism publication-title: J Mol Biol – volume: 462 start-page: 155 year: 1999 end-page: 158 article-title: Molecular electroporation: a unifying concept for the description of membrane pore formation by antibacterial peptides, exemplified with NK‐lysin publication-title: FEBS Lett – volume: 34 start-page: 868 year: 1995 end-page: 878 article-title: Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer publication-title: Biochemistry – volume: 27 start-page: 531 year: 1998 end-page: 539 article-title: acquisition of calcium and expression of CBP1 during intracellular parasitism publication-title: Mol Microbiol – volume: 276 start-page: 27010 year: 2001 end-page: 27017 article-title: Differential membrane interactions of saposins A and C: implications for the functional specificity publication-title: J Biol Chem – volume: 389 start-page: 249 year: 2005 end-page: 257 article-title: A short guided tour through functional and structural features of saposin‐like proteins publication-title: Biochem J – volume: 2 start-page: S53 year: 1997 end-page: S57 article-title: Ambiguous distance data in the calculation of NMR structures publication-title: Fold Des – volume: 16 start-page: 809 year: 2008 end-page: 817 article-title: Crystal structures of human saposins C and D: Implications for lipid recognition and membrane interactions publication-title: Structure – volume: 32 start-page: W582 year: 2004b end-page: W585 article-title: FATCAT: a web server for flexible structure comparison and structure similarity searching publication-title: Nucleic Acids Res – volume: 47 start-page: 4427 year: 2008 end-page: 4438 article-title: Structural features responsible for biological stability of 's virulence factor CBP publication-title: Biochemistry – volume: 115 start-page: 7772 year: 1993 end-page: 7777 article-title: Quantitative J Correlation: a New Approach for Measuring Homonuclear Three‐Bond J (H H ) Coupling Constants in N‐Enriched Proteins publication-title: J Am Chem Soc – volume: 23 start-page: 381 year: 2007 end-page: 382 article-title: ARIA2: automated NOE assignment and data integration in NMR structure calculation publication-title: Bioinformatics – volume: 268 start-page: 18519 year: 1993 end-page: 18523 article-title: Binding of cerebrosides and sulfatides to saposins A‐D publication-title: J Biol Chem – volume: 380 start-page: 1001 year: 1999 end-page: 1007 article-title: Comparative modeling of amoebapores and granulysin based on the NK‐lysin structure‐structural and functional implications publication-title: Biol Chem – volume: 334 start-page: 541 year: 2003 end-page: 549 article-title: Structure of bacteriocin AS‐48: from soluble state to membrane bound state publication-title: J Mol Biol – volume: 11 start-page: 81R year: 2001 end-page: 90R article-title: Sphingolipid activator proteins: proteins with complex functions in lipid degradation and skin biogenesis publication-title: Glycobiology – volume: 443 start-page: 101 year: 2005 end-page: 112 article-title: Role of lysine residues in membrane anchoring of saposin C publication-title: Arch Biochem Biophys – volume: 13 start-page: 289 year: 1999 end-page: 302 article-title: Protein backbone angle restraints from searching a database for chemical shift and sequence homology publication-title: J Biomol NMR – volume: 28 start-page: 8972 year: 1989 end-page: 8979 article-title: Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease publication-title: Biochemistry – volume: 362 start-page: 943 year: 2006 end-page: 953 article-title: Direct visualization of saposin remodelling of lipid bilayers publication-title: J Mol Biol – volume: 18 start-page: 3947 year: 1999 end-page: 3955 article-title: Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting publication-title: EMBO J – volume: 327 start-page: 1121 year: 2003 end-page: 1133 article-title: Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G publication-title: J Mol Biol – volume: 239 start-page: 363 year: 1994b end-page: 392 article-title: Chemical shifts as a tool for structure determination publication-title: Methods Enzymol – volume: 54 start-page: 905 year: 1998 end-page: 921 article-title: Crystallography & NMR system: a new software suite for macromolecular structure determination publication-title: Acta Crystallogr D Biol Crystallogr – volume: 97 start-page: 11221 year: 2000 end-page: 11226 article-title: Bacteriocin AS‐48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK‐lysin publication-title: Proc Natl Acad Sci USA – volume: 339 start-page: 71 year: 2001 end-page: 90 article-title: Automated assignment of ambiguous nuclear overhauser effects with ARIA publication-title: Methods Enzymol – volume: 65 start-page: 5257 year: 1997 end-page: 5261 article-title: Calcium dependence and binding in cultures of publication-title: Infect Immun – volume: 43 start-page: 483 year: 1988 end-page: 491 article-title: Phagosome‐lysosome fusion in P388D1 macrophages infected with publication-title: J Leukoc Biol – volume: 233 start-page: 123 year: 1993 end-page: 138 article-title: Protein structure comparison by alignment of distance matrices publication-title: J Mol Biol – volume: 42 start-page: 14729 year: 2003 end-page: 14740 article-title: Solution structure of human saposin C: pH–dependent interaction with phospholipid vesicles publication-title: Biochemistry – volume: 4 start-page: 793 year: 1997 end-page: 795 article-title: Saposin fold revealed by the NMR structure of NK‐lysin publication-title: Nat Struct Biol – volume: 245 start-page: 645 year: 1995 end-page: 660 article-title: Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities publication-title: J Mol Biol – volume: 276 start-page: 31583 year: 2001 end-page: 31589 article-title: Saposin D solubilizes anionic phospholipid‐containing membranes publication-title: J Biol Chem – volume: 177 start-page: 1605 year: 1993 end-page: 1611 article-title: modulates the acidification of phagolysosomes publication-title: J Exp Med – volume: 14 start-page: 51 year: 1996 end-page: 55 article-title: MOLMOL: a program for display and analysis of macromolecular structures publication-title: J Mol Graph – volume: 26 start-page: 283 year: 1993 end-page: 291 article-title: PROCHECK: a program to check the stereochemical quality of protein structures publication-title: J Appl Cryst – ident: e_1_2_6_12_1 doi: 10.1107/S0907444998003254 – ident: e_1_2_6_36_1 doi: 10.1016/S0022-2275(20)41485-3 – ident: e_1_2_6_41_1 doi: 10.1074/jbc.M101075200 – ident: e_1_2_6_23_1 doi: 10.1073/pnas.210301097 – ident: e_1_2_6_34_1 doi: 10.1016/j.abb.2005.09.007 – ident: e_1_2_6_43_1 doi: 10.1016/j.str.2008.02.016 – ident: e_1_2_6_39_1 doi: 10.1006/jmbi.1997.1044 – ident: e_1_2_6_35_1 doi: 10.1016/S0014-5793(99)01520-3 – ident: e_1_2_6_25_1 doi: 10.1006/jmbi.1993.1489 – ident: e_1_2_6_33_1 doi: 10.1016/S0076-6879(01)39310-2 – ident: e_1_2_6_45_1 doi: 10.1093/glycob/11.6.81R – ident: e_1_2_6_42_1 doi: 10.1093/bioinformatics/btl589 – ident: e_1_2_6_11_1 doi: 10.1515/BC.1999.124 – ident: e_1_2_6_19_1 doi: 10.1084/jem.177.6.1605 – ident: e_1_2_6_5_1 doi: 10.1021/bi0301338 – ident: e_1_2_6_2_1 doi: 10.1073/pnas.0136947100 – ident: e_1_2_6_46_1 doi: 10.1126/science.290.5495.1368 – ident: e_1_2_6_29_1 doi: 10.1016/0263-7855(96)00009-4 – ident: e_1_2_6_3_1 doi: 10.1110/ps.062256606 – ident: e_1_2_6_24_1 doi: 10.1074/jbc.M312978200 – ident: e_1_2_6_30_1 doi: 10.1046/j.1462-5822.2000.00078.x – ident: e_1_2_6_15_1 doi: 10.1023/A:1008392405740 – ident: e_1_2_6_22_1 doi: 10.1093/nar/gkh430 – ident: e_1_2_6_20_1 doi: 10.1021/bi00003a021 – ident: e_1_2_6_21_1 doi: 10.1110/ps.03602304 – ident: e_1_2_6_37_1 doi: 10.1006/jmbi.1994.0053 – ident: e_1_2_6_27_1 doi: 10.1093/emboj/18.14.3947 – ident: e_1_2_6_38_1 doi: 10.1016/S1359-0278(97)00064-3 – ident: e_1_2_6_7_1 doi: 10.1128/IAI.65.12.5257-5261.1997 – ident: e_1_2_6_44_1 doi: 10.1016/j.jmb.2003.09.060 – ident: e_1_2_6_8_1 doi: 10.1046/j.1365-2958.1998.00697.x – volume-title: The PyMOL Molecular Graphics System year: 2002 ident: e_1_2_6_16_1 contributor: fullname: DeLano W.L. – ident: e_1_2_6_52_1 doi: 10.1021/ja970224q – ident: e_1_2_6_13_1 doi: 10.1002/pro.5560050210 – ident: e_1_2_6_28_1 doi: 10.1146/annurev.cellbio.21.122303.120013 – ident: e_1_2_6_9_1 doi: 10.1021/bi701495v – ident: e_1_2_6_32_1 doi: 10.1038/nsb1097-793 – ident: e_1_2_6_49_1 doi: 10.1021/ja00070a024 – ident: e_1_2_6_18_1 doi: 10.1002/jlb.43.6.483 – ident: e_1_2_6_48_1 doi: 10.1016/S0022-2836(03)00238-9 – ident: e_1_2_6_6_1 doi: 10.1016/S0022-2836(02)01234-2 – volume: 268 start-page: 18519 year: 1993 ident: e_1_2_6_47_1 article-title: Binding of cerebrosides and sulfatides to saposins A‐D publication-title: J Biol Chem doi: 10.1016/S0021-9258(17)46658-0 contributor: fullname: Soeda S. – ident: e_1_2_6_31_1 doi: 10.1107/S0021889892009944 – ident: e_1_2_6_50_1 doi: 10.1007/BF00175245 – ident: e_1_2_6_17_1 doi: 10.1021/ja026939x – ident: e_1_2_6_26_1 doi: 10.1021/bi00449a003 – ident: e_1_2_6_4_1 doi: 10.1016/j.jmb.2006.08.009 – ident: e_1_2_6_10_1 doi: 10.1042/BJ20050051 – ident: e_1_2_6_40_1 doi: 10.1016/0958-1669(93)90002-E – ident: e_1_2_6_51_1 doi: 10.1016/S0076-6879(94)39014-2 – ident: e_1_2_6_14_1 doi: 10.1074/jbc.M102736200
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Snippet	The fungal protein CBP ( calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its... Summary The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on... The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its... The fungal protein CBP ( c alcium b inding p rotein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its... SummaryThe fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on...
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SubjectTerms	Amino Acid Sequence Bacterial proteins Binding sites Biological and medical sciences Calcium-Binding Proteins - chemistry Dimerization Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungi Histoplasma - chemistry Histoplasma capsulatum Lipids Microbiology Models, Molecular Molecular Sequence Data NMR Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Conformation Saposins - chemistry Virology Virulence Factors - chemistry
Title	NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B
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