6cbq

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m (Protected "6cbq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6cbq is ON HOLD until Paper Publication
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==Crystal structure of QscR bound to agonist S3==
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<StructureSection load='6cbq' size='340' side='right' caption='[[6cbq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6cbq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CBQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EVY:(2S)-2-hexyl-N-[(3S)-2-oxooxolan-3-yl]decanamide'>EVY</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3szt|3szt]]</td></tr>
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<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=6cbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cbq OCA], [http://pdbe.org/6cbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cbq RCSB], [http://www.ebi.ac.uk/pdbsum/6cbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cbq ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pseudomonas aeruginosa is an opportunistic pathogen that uses the process of quorum sensing (QS) to coordinate the expression of many virulence genes. During quorum sensing, N-acyl-homoserine lactone (AHL) signaling molecules regulate the activity of three LuxR-type transcription factors, LasR, RhlR, and QscR. To better understand P. aeruginosa QS signal reception, we examined the mechanism underlying the response of QscR to synthetic agonists and antagonists using biophysical and structural approaches. The structure of QscR bound to a synthetic agonist reveals a novel mode of ligand binding supporting a general mechanism for agonist activity. In turn, antagonists of QscR with partial agonist activity were found to destabilize and greatly impair QscR dimerization and DNA binding. These results highlight the diversity of LuxR-type receptor responses to small molecule agonists and antagonists and demonstrate the potential for chemical strategies for the selective targeting of individual quorum-sensing systems. This article is protected by copyright. All rights reserved.
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Authors: Churchill, M.E.A., Wysoczynski-Horita, C.L.
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Mechanism of agonism and antagonism of the Pseudomonas aeruginosa quorum sensing regulator QscR with non-native ligands.,Wysoczynski-Horita CL, Boursier ME, Hill R, Hansen K, Blackwell HE, Churchill MEA Mol Microbiol. 2018 Feb 13. doi: 10.1111/mmi.13930. PMID:29437248<ref>PMID:29437248</ref>
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Description: Crystal structure of QscR bound to agonist S3
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Wysoczynski-Horita, C.L]]
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<div class="pdbe-citations 6cbq" style="background-color:#fffaf0;"></div>
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[[Category: Churchill, M.E.A]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Churchill, M E.A]]
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[[Category: Wysoczynski-Horita, C L]]
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[[Category: Luxr-type ahl receptor]]
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[[Category: Pseudomonas aeruginosa qscr]]
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[[Category: Transcription]]
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[[Category: Transcription-agonist complex]]

Revision as of 06:36, 28 February 2018

Crystal structure of QscR bound to agonist S3

6cbq, resolution 2.80Å

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