8gsy
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of Clostridium perfringens pili protein B N-terminal domain== | |
| + | <StructureSection load='8gsy' size='340' side='right'caption='[[8gsy]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8gsy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GSY FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8gsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gsy OCA], [https://pdbe.org/8gsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gsy RCSB], [https://www.ebi.ac.uk/pdbsum/8gsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gsy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A2X3IRB0_CLOPF A0A2X3IRB0_CLOPF] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sortase-mediated pili are flexible rod proteins composed of major and minor/tip pilins, playing important roles in the initial adhesion of bacterial cells to host tissues. The pilus shaft is formed by covalent polymerization of major pilins, and the minor/tip pilin is covalently attached to the tip of the shaft involved in adhesion to the host cell. The Gram-positive bacterium Clostridium perfringens has a major pilin, and a minor/tip pilin (CppB) with the collagen-binding motif. Here, we report X-ray structures of CppB collagen-binding domains, collagen-binding assays and mutagenesis analysis, demonstrating that CppB collagen-binding domains adopt an L-shaped structure in open form, and that a small beta-sheet unique to CppB provides a scaffold for a favourable binding site for collagen peptide. | ||
| - | + | Structural and biochemical characterization of Clostridium perfringens pili protein B collagen-binding domains.,Tamai E, Yamada M, Ishida T, Arimura N, Matsunami R, Sekiya H, Kamitori S FEBS Lett. 2023 May;597(10):1345-1354. doi: 10.1002/1873-3468.14626. Epub 2023 , Apr 27. PMID:37071018<ref>PMID:37071018</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8gsy" style="background-color:#fffaf0;"></div> |
| - | [[Category: Tamai | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridium perfringens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kamitori S]] | ||
| + | [[Category: Tamai E]] | ||
| + | [[Category: Yamada M]] | ||
Revision as of 05:42, 7 June 2023
X-ray structure of Clostridium perfringens pili protein B N-terminal domain
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