5WQW

X-ray structure of catalytic domain of autolysin from Clostridium perfringens

「5AZM」から置き換えられました

5WQW の概要

• エントリーDOI: 10.2210/pdb5wqw/pdb
• 分子名称: N-acetylglucosaminidase, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: autolysin, glycoside hydrolase 73 family, hydrolase
• 由来する生物種: Clostridium perfringens (strain 13 / Type A)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30948.74

構造登録者

Tamai, E.,Sekiya, H.,Goda, E.,Makihata, N.,Maki, J.,Yoshida, H.,Kamitori, S. (登録日: 2016-11-29, 公開日: 2016-12-07, 最終更新日: 2024-03-20)

主引用文献

Tamai, E.,Sekiya, H.,Goda, E.,Makihata, N.,Maki, J.,Yoshida, H.,Kamitori, S.
Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain
FEBS Lett., 591:231-239, 2017

PubMed Abstract: Bacterial autolysins can partially hydrolyze cell wall peptidoglycans into small sections to regulate cell separation/division and the growth phase. Clostridium perfringens autolysin (Acp) has an N-terminal cell wall-binding domain and a C-terminal catalytic domain with glucosaminidase activity that belongs to the glycoside hydrolase 73 family. Here, we determined the X-ray structure of the Acp catalytic domain (AcpCD) at 1.76 Å resolution. AcpCD has a unique crescent-shaped structure, forming a deep groove for substrate-binding at the center of the protein. The modeling study of the enzyme/substrate complex demonstrated that the length of the substrate-binding groove is closely related to the glucosaminidase activity. Mutagenesis analysis showed that AcpCD likely adopts a neighboring-group mechanism for the catalytic reaction.

PubMed: 27926788
DOI: 10.1002/1873-3468.12515

実験手法

X-RAY DIFFRACTION (1.76 Å)