1y08
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1y08 |SIZE=350|CAPTION= <scene name='initialview01'>1y08</scene>, resolution 1.93Å | |PDB= 1y08 |SIZE=350|CAPTION= <scene name='initialview01'>1y08</scene>, resolution 1.93Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y08 OCA], [http://www.ebi.ac.uk/pdbsum/1y08 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y08 RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Sondermann, P.]] | [[Category: Sondermann, P.]] | ||
[[Category: Wenig, K.]] | [[Category: Wenig, K.]] | ||
| - | [[Category: SO4]] | ||
[[Category: cysteine proteinase]] | [[Category: cysteine proteinase]] | ||
[[Category: papain-like fold with major insertion]] | [[Category: papain-like fold with major insertion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:57:03 2008'' |
Revision as of 21:57, 30 March 2008
| |||||||
| , resolution 1.93Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 00:57:03 2008
