8GSY
X-ray structure of Clostridium perfringens pili protein B N-terminal domain
Summary for 8GSY
| Entry DOI | 10.2210/pdb8gsy/pdb |
| Descriptor | Peptidoglycan bound protein (2 entities in total) |
| Functional Keywords | pili protein, protein fibril |
| Biological source | Clostridium perfringens |
| Total number of polymer chains | 2 |
| Total formula weight | 32736.92 |
| Authors | Kamitori, S.,Yamada, M.,Tamai, E. (deposition date: 2022-09-07, release date: 2023-06-07, Last modification date: 2023-11-29) |
| Primary citation | 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., 597:1345-1354, 2023 Cited by PubMed Abstract: 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 β-sheet unique to CppB provides a scaffold for a favourable binding site for collagen peptide. PubMed: 37071018DOI: 10.1002/1873-3468.14626 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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