1y08: Difference between revisions
New page: left|200px<br /><applet load="1y08" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y08, resolution 1.93Å" /> '''Structure of the Str... |
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[[Image:1y08.gif|left|200px]]<br /><applet load="1y08" size=" | [[Image:1y08.gif|left|200px]]<br /><applet load="1y08" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1y08, resolution 1.93Å" /> | caption="1y08, resolution 1.93Å" /> | ||
'''Structure of the Streptococcal Endopeptidase IdeS, a Novel Cysteine Proteinase with Strict Specificity for IgG'''<br /> | '''Structure of the Streptococcal Endopeptidase IdeS, a Novel Cysteine Proteinase with Strict Specificity for IgG'''<br /> | ||
==Overview== | ==Overview== | ||
Pathogenic bacteria have developed complex and diverse virulence | 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== | ==About this Structure== | ||
1Y08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1Y08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y08 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Chatwell, L.]] | [[Category: Chatwell, L.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Pawel-Rammingen, U | [[Category: Pawel-Rammingen, U von.]] | ||
[[Category: Sondermann, P.]] | [[Category: Sondermann, P.]] | ||
[[Category: Wenig, K.]] | [[Category: Wenig, K.]] | ||
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[[Category: papain-like fold with major insertions]] | [[Category: papain-like fold with major insertions]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:36 2008'' | ||
Revision as of 14:00, 21 February 2008
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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
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