5A0R

Product peptide-bound structure of metalloprotease Zmp1 variant E143A from Clostridium difficile

5A0R の概要

• エントリーDOI: 10.2210/pdb5a0r/pdb
• 関連するPDBエントリー: 5A0P 5A0S 5A0X
• 分子名称: ZINC METALLOPROTEASE ZMP1, PRODUCT PEPTIDE, ZINC ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, metalloprotease, zmp1, proline specificity
• 由来する生物種: CLOSTRIDIUM DIFFICILE; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 45317.52

構造登録者

Schacherl, M.,Pichlo, C.,Neundorf, I.,Baumann, U. (登録日: 2015-04-22, 公開日: 2015-08-05, 最終更新日: 2024-11-13)

主引用文献

Schacherl, M.,Pichlo, C.,Neundorf, I.,Baumann, U.
Structural Basis of Proline-Proline Peptide Bond Specificity of the Metalloprotease Zmp1 Implicated in Motility of Clostridium Difficile.
Structure, 23:1632-, 2015

PubMed Abstract: Clostridium difficile is a pathogenic bacterium causing gastrointestinal diseases from mild diarrhea to toxic megacolon. In common with other pathogenic bacteria, C. difficile secretes proteins involved in adhesion, colonization, and dissemination. The recently identified Zmp1 is an extracellular metalloprotease showing a unique specificity for Pro-Pro peptide bonds. The endogenous substrates of Zmp1 are two surface proteins implicated in adhesion of C. difficile to surface proteins of human cells. Thus, Zmp1 is believed to be involved in the regulation of the adhesion-motility balance of C. difficile. Here, we report crystal structures of Zmp1 from C. difficile in its unbound and peptide-bound forms. The structure analysis revealed a fold similar to Bacillus anthracis lethal factor. Crystal structures in the open and closed conformation of the S-loop shed light on the mode of binding of the substrate, and reveal important residues for substrate recognition and the strict specificity of Zmp1 for Pro-Pro peptide bonds.

PubMed: 26211609
DOI: 10.1016/J.STR.2015.06.018

実験手法

X-RAY DIFFRACTION (1.251 Å)