2y6t: Difference between revisions
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< | ==Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis== | ||
<StructureSection load='2y6t' size='340' side='right'caption='[[2y6t]], [[Resolution|resolution]] 2.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2y6t]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis_YPIII Yersinia pseudotuberculosis YPIII]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y6T 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]] 2.74Å</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=2y6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y6t OCA], [https://pdbe.org/2y6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y6t RCSB], [https://www.ebi.ac.uk/pdbsum/2y6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y6t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Resistance to antibiotics is a problem not only in terms of healthcare but also biodefense. Engineering of resistance into a human pathogen could create an untreatable biothreat pathogen. One such pathogen is Yersinia pestis, the causative agent of plague. Previously, we have used a bioinformatic approach to identify proteins that may be suitable targets for antimicrobial therapy and in particular for the treatment of plague. The serine protease inhibitor ecotin was identified as one such target. We have carried out mutational analyses in the closely related Yersinia pseudotuberculosis, validating that the ecotin gene is a virulence-associated gene in this bacterium. Y. pestis ecotin inhibits chymotrypsin. Here, we present the structure of ecotin in complex with chymotrypsin to 2.74 A resolution. The structure features a biologically relevant tetramer whereby an ecotin dimer binds to two chymotrypsin molecules, similar to what was observed in related serine protease inhibitor structures. However, the vast majority of the interactions in the present structure are distinctive, indicating that the broad specificity of the inhibitor for these proteases is based largely on its capacity to recognize features unique to each of them. These findings will have implications for the development of small ecotin inhibitors for therapeutic use. | |||
Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis.,Clark EA, Walker N, Ford DC, Cooper IA, Oyston PC, Acharya KR J Biol Chem. 2011 Jul 8;286(27):24015-22. Epub 2011 Apr 29. PMID:21531711<ref>PMID:21531711</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2y6t" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]] | ||
*[[Ecotin|Ecotin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Yersinia pseudotuberculosis]] | [[Category: Yersinia pseudotuberculosis YPIII]] | ||
[[Category: Acharya | [[Category: Acharya KR]] | ||
[[Category: Clark | [[Category: Clark EA]] | ||
[[Category: Cooper | [[Category: Cooper IA]] | ||
[[Category: Ford | [[Category: Ford DC]] | ||
[[Category: Oyston | [[Category: Oyston PCF]] | ||
[[Category: Walker | [[Category: Walker N]] | ||
Latest revision as of 13:46, 20 December 2023
Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestisMolecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis
Structural highlights
FunctionPublication Abstract from PubMedResistance to antibiotics is a problem not only in terms of healthcare but also biodefense. Engineering of resistance into a human pathogen could create an untreatable biothreat pathogen. One such pathogen is Yersinia pestis, the causative agent of plague. Previously, we have used a bioinformatic approach to identify proteins that may be suitable targets for antimicrobial therapy and in particular for the treatment of plague. The serine protease inhibitor ecotin was identified as one such target. We have carried out mutational analyses in the closely related Yersinia pseudotuberculosis, validating that the ecotin gene is a virulence-associated gene in this bacterium. Y. pestis ecotin inhibits chymotrypsin. Here, we present the structure of ecotin in complex with chymotrypsin to 2.74 A resolution. The structure features a biologically relevant tetramer whereby an ecotin dimer binds to two chymotrypsin molecules, similar to what was observed in related serine protease inhibitor structures. However, the vast majority of the interactions in the present structure are distinctive, indicating that the broad specificity of the inhibitor for these proteases is based largely on its capacity to recognize features unique to each of them. These findings will have implications for the development of small ecotin inhibitors for therapeutic use. Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis.,Clark EA, Walker N, Ford DC, Cooper IA, Oyston PC, Acharya KR J Biol Chem. 2011 Jul 8;286(27):24015-22. Epub 2011 Apr 29. PMID:21531711[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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