5ep2

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<StructureSection load='5ep2' size='340' side='right'caption='[[5ep2]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
<StructureSection load='5ep2' size='340' side='right'caption='[[5ep2]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ep2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25915 Atcc 25915]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EP2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ep2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Photobacterium_angustum Photobacterium angustum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EP2 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AZU:2,2-DIMETHYLPROPYL+2-[[3,5-BIS(OXIDANYLIDENE)-2~{H}-1,2,4-TRIAZIN-6-YL]SULFANYL]ETHANOATE'>AZU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.421&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ep0|5ep0]], [[5ep1|5ep1]], [[5ep3|5ep3]], [[5ep4|5ep4]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AZU:2,2-DIMETHYLPROPYL+2-[[3,5-BIS(OXIDANYLIDENE)-2~{H}-1,2,4-TRIAZIN-6-YL]SULFANYL]ETHANOATE'>AZU</scene></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=5ep2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ep2 OCA], [http://pdbe.org/5ep2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ep2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ep2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ep2 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ep2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ep2 OCA], [https://pdbe.org/5ep2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ep2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ep2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ep2 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q1ZS18_PHOAS Q1ZS18_PHOAS]
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In a process called quorum sensing, bacteria communicate with chemical signal molecules called autoinducers to control collective behaviors. In pathogenic vibrios, including Vibrio cholerae, the accumulation of autoinducers triggers repression of genes responsible for virulence factor production and biofilm formation. The vibrio autoinducer molecules bind to transmembrane receptors of the two-component histidine sensor kinase family. Autoinducer binding inactivates the receptors' kinase activities, leading to dephosphorylation and inhibition of the downstream response regulator LuxO. Here, we report the X-ray structure of LuxO in its unphosphorylated, autoinhibited state. Our structure reveals that LuxO, a bacterial enhancer-binding protein of the AAA+ ATPase superfamily, is inhibited by an unprecedented mechanism in which a linker that connects the catalytic and regulatory receiver domains occupies the ATPase active site. The conformational change that accompanies receiver domain phosphorylation likely disrupts this interaction, providing a mechanistic rationale for LuxO activation. We also determined the crystal structure of the LuxO catalytic domain bound to a broad-spectrum inhibitor. The inhibitor binds in the ATPase active site and recapitulates elements of the natural regulatory mechanism. Remarkably, a single inhibitor molecule may be capable of inhibiting an entire LuxO oligomer.
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Structure, Regulation, and Inhibition of the Quorum-Sensing Signal Integrator LuxO.,Boyaci H, Shah T, Hurley A, Kokona B, Li Z, Ventocilla C, Jeffrey PD, Semmelhack MF, Fairman R, Bassler BL, Hughson FM PLoS Biol. 2016 May 24;14(5):e1002464. doi: 10.1371/journal.pbio.1002464., eCollection 2016 May. PMID:27219477<ref>PMID:27219477</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5ep2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 25915]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hughson, F M]]
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[[Category: Photobacterium angustum]]
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[[Category: Jeffrey, P D]]
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[[Category: Hughson FM]]
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[[Category: Selcuk, H B]]
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[[Category: Jeffrey PD]]
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[[Category: Shah, T]]
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[[Category: Selcuk HB]]
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[[Category: Aaa+ protein]]
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[[Category: Shah T]]
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[[Category: Atpase]]
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[[Category: Catalytic domain]]
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[[Category: Inhibitor]]
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[[Category: Quorum sensing]]
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[[Category: Transcription-transcription inhibitor complex]]
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Current revision

Quorum-Sensing Signal Integrator LuxO - Catalytic Domain in Complex with AzaU Inhibitor

PDB ID 5ep2

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Proteopedia Page Contributors and Editors (what is this?)

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