5JIP

Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM

5JIP の概要

• エントリーDOI: 10.2210/pdb5jip/pdb
• 分子名称: Cortical-lytic enzyme, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: spore, cortex, peptidoglycan-lysin, hydrolase
• 由来する生物種: Clostridium perfringens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75998.21

構造登録者

Chirgadze, D.Y.,Christie, G.,Ustok, F.I.,Al-Riyami, B.,Stott, K. (登録日: 2016-04-22, 公開日: 2016-08-10, 最終更新日: 2024-01-10)

主引用文献

Al-Riyami, B.,Ustok, F.I.,Stott, K.,Chirgadze, D.Y.,Christie, G.
The crystal structure of Clostridium perfringens SleM, a muramidase involved in cortical hydrolysis during spore germination.
Proteins, 84:1681-1689, 2016

PubMed Abstract: Clostridium perfringens spores employ two peptidoglycan lysins to degrade the spore cortex during germination. SleC initiates cortex hydrolysis to generate cortical fragments that are degraded further by the muramidase SleM. Here, we present the crystal structure of the C. perfringens S40 SleM protein at 1.8 Å. SleM comprises an N-terminal catalytic domain that adopts an irregular α/β-barrel fold that is common to GH25 family lysozymes, plus a C-terminal fibronectin type III domain. The latter is involved in forming the SleM dimer that is evident in both the crystal structure and in solution. A truncated form of SleM that lacks the FnIII domain shows reduced activity against spore sacculi indicating that this domain may have a role in facilitating the position of substrate with respect to the enzyme's active site. Proteins 2016; 84:1681-1689. © 2016 Wiley Periodicals, Inc.

PubMed: 27488615
DOI: 10.1002/prot.25112

実験手法

X-RAY DIFFRACTION (1.8 Å)