8gsx | pdb_00008gsx

X-ray structure of Clostridium perfringens pili protein B collagen-binding domains

spinqualitylabelsall models 8gsx, resolution 2.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8gsx is a 1 chain structure with sequence from Clostridium perfringens str. 13. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8XP11_CLOPE 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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