PMID:15574492
| Citation |
Wenig, K, Chatwell, L, von Pawel-Rammingen, U, Björck, L, Huber, R and Sondermann, P (2004) Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG. Proc. Natl. Acad. Sci. U.S.A. 101:17371-6 |
|---|---|
| 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. |
| Links |
PubMed PMC536041 Online version:10.1073/pnas.0407965101 |
| Keywords |
Amino Acid Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; Cysteine/genetics; Cysteine/metabolism; Cysteine Endopeptidases/chemistry; Cysteine Endopeptidases/genetics; Cysteine Endopeptidases/metabolism; Immunoglobulin Fc Fragments/chemistry; Immunoglobulin Fc Fragments/metabolism; Immunoglobulin G/chemistry; Immunoglobulin G/metabolism; Models, Molecular; Molecular Sequence Data; Papain/chemistry; Papain/metabolism; Protein Structure, Tertiary; Sequence Alignment; Streptococcus pyogenes/enzymology; Streptococcus pyogenes/genetics; Substrate Specificity |
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