2y6t

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Revision as of 11:49, 5 August 2016

Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis

Structural highlights

2y6t is a 8 chain structure with sequence from Bovin and Yerpy. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2gct, 4vgc, 1gcd, 1mtn, 1gmh, 8gch, 1t8n, 1gct, 1gg6, 1t8o, 3gct, 5cha, 1p2q, 1ab9, 1gl1, 2vgc, 2cga, 1cgj, 1cho, 1cbw, 2gmt, 1ghb, 6gch, 1k2i, 1gha, 3vgc, 7gch, 3gch, 1cgi, 4gch, 1gmc, 1ca0, 1afq, 1oxg, 1gl0, 1chg, 1ggd, 2gch, 1t7c, 1yph, 1p2o, 1dlk, 1p2n, 1n8o, 1t8m, 1gmd, 4cha, 5gch, 1ex3, 1p2m, 1vgc, 1t8l, 2cha, 1hja, 6cha, 1acb
Activity:	Chymotrypsin, with EC number 3.4.21.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ECOT_YERPY] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases (By similarity).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Clark EA, Walker N, Ford DC, Cooper IA, Oyston PC, Acharya KR. Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis. J Biol Chem. 2011 Jul 8;286(27):24015-22. Epub 2011 Apr 29. PMID:21531711 doi:10.1074/jbc.M111.225730

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2y6t"

@@ Line 1: / Line 1: @@
 ==Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis==
 <StructureSection load='2y6t' size='340' side='right' caption='[[2y6t]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gct|2gct]], [[4vgc|4vgc]], [[1gcd|1gcd]], [[1mtn|1mtn]], [[1gmh|1gmh]], [[8gch|8gch]], [[1t8n|1t8n]], [[1gct|1gct]], [[1gg6|1gg6]], [[1t8o|1t8o]], [[3gct|3gct]], [[5cha|5cha]], [[1p2q|1p2q]], [[1ab9|1ab9]], [[1gl1|1gl1]], [[2vgc|2vgc]], [[2cga|2cga]], [[1cgj|1cgj]], [[1cho|1cho]], [[1cbw|1cbw]], [[2gmt|2gmt]], [[1ghb|1ghb]], [[6gch|6gch]], [[1k2i|1k2i]], [[1gha|1gha]], [[3vgc|3vgc]], [[7gch|7gch]], [[3gch|3gch]], [[1cgi|1cgi]], [[4gch|4gch]], [[1gmc|1gmc]], [[1ca0|1ca0]], [[1afq|1afq]], [[1oxg|1oxg]], [[1gl0|1gl0]], [[1chg|1chg]], [[1ggd|1ggd]], [[2gch|2gch]], [[1t7c|1t7c]], [[1yph|1yph]], [[1p2o|1p2o]], [[1dlk|1dlk]], [[1p2n|1p2n]], [[1n8o|1n8o]], [[1t8m|1t8m]], [[1gmd|1gmd]], [[4cha|4cha]], [[5gch|5gch]], [[1ex3|1ex3]], [[1p2m|1p2m]], [[1vgc|1vgc]], [[1t8l|1t8l]], [[2cha|2cha]], [[1hja|1hja]], [[6cha|6cha]], [[1acb|1acb]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y6t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y6t RCSB], [http://www.ebi.ac.uk/pdbsum/2y6t PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y6t OCA], [http://pdbe.org/2y6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y6t RCSB], [http://www.ebi.ac.uk/pdbsum/2y6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y6t ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2y6t" style="background-color:#fffaf0;"></div>
 ==See Also==

2y6t

From Proteopedia

Revision as of 11:49, 5 August 2016

Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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