5XCC

X-ray structure of Clostridium perfringens pili protein CppA

5XCC の概要

• エントリーDOI: 10.2210/pdb5xcc/pdb
• 関連するPDBエントリー: 5XCB
• 分子名称: Probable surface protein (2 entities in total)
• 機能のキーワード: pili protein, structural protein
• 由来する生物種: Clostridium perfringens str. 13
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104758.02

構造登録者

Kamitori, S.,Tamai, E. (登録日: 2017-03-22, 公開日: 2018-02-28, 最終更新日: 2024-11-06)

主引用文献

Tamai, E.,Katayama, S.,Sekiya, H.,Nariya, H.,Kamitori, S.
Structures of major pilins in Clostridium perfringens demonstrate dynamic conformational change.
Acta Crystallogr D Struct Biol, 75:718-732, 2019

PubMed Abstract: Pili in Gram-positive bacteria are flexible rod proteins associated with the bacterial cell surface, and they play important roles in the initial adhesion to host tissues and colonization. The pilus shaft is formed by the covalent polymerization of major pilins, catalyzed by sortases, a family of cysteine transpeptidases. Here, X-ray structures of the major pilins from Clostridium perfringens strains 13 and SM101 and of sortase from strain SM101 are presented with biochemical analysis to detect the formation of pili in vivo. The major pilin from strain 13 adopts an elongated structure to form noncovalently linked polymeric chains in the crystal, yielding a practical model of the pilus fiber structure. The major pilin from strain SM101 adopts a novel bent structure and associates to form a left-handed twist like an antiparallel double helix in the crystal, which is likely to promote bacterial cell-cell interactions. A modeling study showed that pilin with a bent structure interacts favorably with sortase. The major pilin from strain SM101 was considered to be in an equilibrium state between an elongated and a bent structure through dynamic conformational change, which may be involved in pili-mediated colonization and sortase-mediated polymerization of pili.

PubMed: 31373571
DOI: 10.1107/S2059798319009689

実験手法

X-RAY DIFFRACTION (2.48 Å)