8gsx
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==X-ray structure of Clostridium perfringens pili protein B collagen-binding domains== | |
+ | <StructureSection load='8gsx' size='340' side='right'caption='[[8gsx]], [[Resolution|resolution]] 2.86Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[8gsx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_str._13 Clostridium perfringens str. 13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GSX FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=8gsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gsx OCA], [https://pdbe.org/8gsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gsx RCSB], [https://www.ebi.ac.uk/pdbsum/8gsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gsx ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q8XP11_CLOPE Q8XP11_CLOPE] | ||
+ | <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 8gsx" style="background-color:#fffaf0;"></div> |
- | [[Category: Tamai | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Clostridium perfringens str. 13]] | ||
+ | [[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 collagen-binding domains
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