8GSX

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

Summary for 8GSX

• Entry DOI: 10.2210/pdb8gsx/pdb
• Descriptor: pili protein, ACETATE ION (3 entities in total)
• Functional Keywords: pili, protein fibril
• Biological source: Clostridium perfringens
• Total number of polymer chains: 1
• Total formula weight: 38704.09

Authors

Kamitori, S.,Yamada, M.,Tamai, E. (deposition date: 2022-09-07, release date: 2023-06-07, Last modification date: 2024-05-29)

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

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: 37071018
DOI: 10.1002/1873-3468.14626

Experimental method

X-RAY DIFFRACTION (2.86 Å)