From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1y08, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1Y08 is a Single protein structure of sequence from Streptococcus pyogenes with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG., Wenig K, Chatwell L, von Pawel-Rammingen U, Bjorck L, Huber R, Sondermann P, Proc Natl Acad Sci U S A. 2004 Dec 14;101(50):17371-6. Epub 2004 Dec 1. PMID:15574492

Page seeded by OCA on Sun Nov 25 03:16:00 2007