1Y08

Structure of the Streptococcal Endopeptidase IdeS, a Novel Cysteine Proteinase with Strict Specificity for IgG

1Y08 の概要

• エントリーDOI: 10.2210/pdb1y08/pdb
• 分子名称: hypothetical protein SPy0861, SULFATE ION (3 entities in total)
• 機能のキーワード: cysteine proteinase, papain-like fold with major insertions, hydrolase
• 由来する生物種: Streptococcus pyogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36489.74

構造登録者

Wenig, K.,Chatwell, L.,von Pawel-Rammingen, U.,Bjoerck, L.,Huber, R.,Sondermann, P. (登録日: 2004-11-15, 公開日: 2004-12-21, 最終更新日: 2024-05-29)

主引用文献

Wenig, K.,Chatwell, L.,von Pawel-Rammingen, U.,Bjoerck, L.,Huber, R.,Sondermann, P.
Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG
Proc.Natl.Acad.Sci.Usa, 101:17371-17376, 2004

PubMed Abstract: Pathogenic bacteria have developed complex and diverse virulence mechanisms that weaken or disable the host immune defense system. IdeS (IgG-degrading enzyme of Streptococcus pyogenes) is a secreted cysteine endopeptidase from the human pathogen S. pyogenes with an extraordinarily high degree of substrate specificity, catalyzing a single proteolytic cleavage at the lower hinge of human IgG. This proteolytic degradation promotes inhibition of opsonophagocytosis and interferes with the killing of group A Streptococcus. We have determined the crystal structure of the catalytically inactive mutant IdeS-C94S by x-ray crystallography at 1.9-A resolution. Despite negligible sequence homology to known proteinases, the core of the structure resembles the canonical papain fold although with major insertions and a distinct substrate-binding site. Therefore IdeS belongs to a unique family within the CA clan of cysteine proteinases. Based on analogy with inhibitor complexes of papain-like proteinases, we propose a model for substrate binding by IdeS.

PubMed: 15574492
DOI: 10.1073/pnas.0407965101

実験手法

X-RAY DIFFRACTION (1.93 Å)