7D6T

X-ray structure of Clostridium perfringens sortase C with the C-terminal cell wall sorting motif.

7D6T の概要

• エントリーDOI: 10.2210/pdb7d6t/pdb
• 関連するPDBエントリー: 6IXZ
• 分子名称: Sortase family protein (2 entities in total)
• 機能のキーワード: cysteine transpeptidase, transferase
• 由来する生物種: Clostridium perfringens (strain SM101 / Type A)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49661.92

構造登録者

Kamitori, S.,Tamai, E. (登録日: 2020-10-01, 公開日: 2021-06-02, 最終更新日: 2023-11-29)

主引用文献

Tamai, E.,Sekiya, H.,Nariya, H.,Katayama, S.,Kamitori, S.
X-ray structures of Clostridium perfringens sortase C with C-terminal cell wall sorting motif of LPST demonstrate role of subsite for substrate-binding and structural variations of catalytic site.
Biochem.Biophys.Res.Commun., 554:138-144, 2021

PubMed Abstract: Pili of Gram-positive bacteria are flexible rod proteins covalently attached to the bacterial cell wall, that play important roles in the initial adhesion of bacterial cells to host tissues and bacterial colonization. Pili are formed by the polymerization of major and minor pilins, catalyzed by class C sortase (SrtC), a family of cysteine transpeptidases. The Gram-positive bacterium Clostridium perfringens has a major pilin (CppA), a minor pilin (CppB), and SrtC (CpSrtC). CpSrtC recognizes the C-terminal cell wall sorting signal motifs with five amino acid residues, LPSTG of CppA and LPETG of CppB, for the polymerization of pili. Here, we report biochemical analysis to detect the formation of Clostridium perfringens pili in vivo, and the X-ray structure of a novel intermolecular substrate-enzyme complex of CpSrtC with a sequence of LPST at the C-terminal site. The results showed that CpSrtC has a subsite for substrate-binding to aid polymerization of pili, and that the catalytic site has structural variations, giving insights into the enzyme catalytic reaction mechanism and affinities for the C-terminal cell wall sorting signal motif sequences.

PubMed: 33794418
DOI: 10.1016/j.bbrc.2021.03.106

実験手法

X-RAY DIFFRACTION (1.68 Å)