Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tamai E, Yamada M, Ishida T, Arimura N, Matsunami R, Sekiya H, Kamitori S. Structural and biochemical characterization of Clostridium perfringens pili protein B collagen-binding domains. FEBS Lett. 2023 May;597(10):1345-1354. PMID:37071018 doi:10.1002/1873-3468.14626
