1y08: Difference between revisions
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==Structure of the Streptococcal Endopeptidase IdeS, a Novel Cysteine Proteinase with Strict Specificity for IgG== | |||
<StructureSection load='1y08' size='340' side='right'caption='[[1y08]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1y08]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y08 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y08 OCA], [https://pdbe.org/1y08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y08 RCSB], [https://www.ebi.ac.uk/pdbsum/1y08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y08 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9F1R7_STRPY Q9F1R7_STRPY] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y0/1y08_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y08 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:15574492</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1y08" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Streptococcus pyogenes]] | [[Category: Streptococcus pyogenes]] | ||
[[Category: Bjoerck | [[Category: Bjoerck L]] | ||
[[Category: Chatwell | [[Category: Chatwell L]] | ||
[[Category: Huber | [[Category: Huber R]] | ||
[[Category: Sondermann P]] | |||
[[Category: Sondermann | [[Category: Wenig K]] | ||
[[Category: Wenig | [[Category: Von Pawel-Rammingen U]] | ||
[[Category: | |||
Latest revision as of 10:59, 15 May 2024
Structure of the Streptococcal Endopeptidase IdeS, a Novel Cysteine Proteinase with Strict Specificity for IgGStructure of the Streptococcal Endopeptidase IdeS, a Novel Cysteine Proteinase with Strict Specificity for IgG
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPathogenic 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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