5kew

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m (Protected "5kew" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5kew is ON HOLD
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==Vibrio parahaemolyticus VtrA/VtrC complex bound to the bile salt taurodeoxycholate==
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<StructureSection load='5kew' size='340' side='right' caption='[[5kew]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5kew]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KEW 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=6SB:TAURODEOXYCHOLATE'>6SB</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kev|5kev]]</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=5kew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kew OCA], [http://pdbe.org/5kew PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kew RCSB], [http://www.ebi.ac.uk/pdbsum/5kew PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kew 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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Bile is an important component of the human gastrointestinal tract with an essential role in food absorption and antimicrobial activities. Enteric bacterial pathogens have developed strategies to sense bile as an environmental cue to regulate virulence genes during infection. We discovered that Vibrio parahaemolyticus VtrC, along with VtrA and VtrB, are required for activating the virulence type III secretion system 2 in response to bile salts. The VtrA/VtrC complex activates VtrB in the presence of bile salts. The crystal structure of the periplasmic domains of the VtrA/VtrC heterodimer reveals a beta-barrel with a hydrophobic inner chamber. A co-crystal structure of VtrA/VtrC with bile salt, along with biophysical and mutational analysis, demonstrates that the hydrophobic chamber binds bile salts and activates the virulence network. As part of a family of conserved signaling receptors, VtrA/VtrC provides structural and functional insights into the evolutionarily conserved mechanism used by bacteria to sense their environment.
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Authors:
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Bile salt receptor complex activates a pathogenic type III secretion system.,Li P, Rivera-Cancel G, Kinch LN, Salomon D, Tomchick DR, Grishin NV, Orth K Elife. 2016 Jul 5;5. pii: e15718. doi: 10.7554/eLife.15718. PMID:27377244<ref>PMID:27377244</ref>
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Description:
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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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<div class="pdbe-citations 5kew" style="background-color:#fffaf0;"></div>
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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: Orth, K]]
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[[Category: Rivera-Cancel, G]]
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[[Category: Tomchick, D R]]
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[[Category: Alpha/beta]]
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[[Category: Bile salt receptor]]
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[[Category: Calycin beta barrel superfamily]]
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[[Category: Heterodimer]]
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[[Category: Signaling protein]]
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[[Category: Taurodeoxycholate]]

Revision as of 15:18, 26 July 2016

Vibrio parahaemolyticus VtrA/VtrC complex bound to the bile salt taurodeoxycholate

5kew, resolution 2.10Å

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