5J72

Cwp6 from Clostridium difficile

5J72 の概要

• エントリーDOI: 10.2210/pdb5j72/pdb
• 分子名称: Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6, CALCIUM ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: amidase_3, cwb2 domain, cell wall protein, s-layer, hydrolase
• 由来する生物種: Peptoclostridium difficile (strain 630); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 139601.18

構造登録者

Renko, M.,Usenik, A.,Turk, D. (登録日: 2016-04-05, 公開日: 2017-02-08, 最終更新日: 2024-01-10)

主引用文献

Usenik, A.,Renko, M.,Mihelic, M.,Lindic, N.,Borisek, J.,Perdih, A.,Pretnar, G.,Muller, U.,Turk, D.
The CWB2 Cell Wall-Anchoring Module Is Revealed by the Crystal Structures of the Clostridium difficile Cell Wall Proteins Cwp8 and Cwp6.
Structure, 25:514-521, 2017

PubMed Abstract: Bacterial cell wall proteins play crucial roles in cell survival, growth, and environmental interactions. In Gram-positive bacteria, cell wall proteins include several types that are non-covalently attached via cell wall binding domains. Of the two conserved surface-layer (S-layer)-anchoring modules composed of three tandem SLH or CWB2 domains, the latter have so far eluded structural insight. The crystal structures of Cwp8 and Cwp6 reveal multi-domain proteins, each containing an embedded CWB2 module. It consists of a triangular trimer of Rossmann-fold CWB2 domains, a feature common to 29 cell wall proteins in Clostridium difficile 630. The structural basis of the intact module fold necessary for its binding to the cell wall is revealed. A comparison with previously reported atomic force microscopy data of S-layers suggests that C. difficile S-layers are complex oligomeric structures, likely composed of several different proteins.

PubMed: 28132783
DOI: 10.1016/j.str.2016.12.018

実験手法

X-RAY DIFFRACTION (1.7 Å)