1Y08
Structure of the Streptococcal Endopeptidase IdeS, a Novel Cysteine Proteinase with Strict Specificity for IgG
Summary for 1Y08
| Entry DOI | 10.2210/pdb1y08/pdb |
| Descriptor | hypothetical protein SPy0861, SULFATE ION (3 entities in total) |
| Functional Keywords | cysteine proteinase, papain-like fold with major insertions, hydrolase |
| Biological source | Streptococcus pyogenes |
| Total number of polymer chains | 1 |
| Total formula weight | 36489.74 |
| Authors | Wenig, K.,Chatwell, L.,von Pawel-Rammingen, U.,Bjoerck, L.,Huber, R.,Sondermann, P. (deposition date: 2004-11-15, release date: 2004-12-21, Last modification date: 2024-05-29) |
| Primary citation | 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 Cited by 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: 15574492DOI: 10.1073/pnas.0407965101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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