3o1h: Difference between revisions

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New page: '''Unreleased structure''' The entry 3o1h is ON HOLD Authors: Moore, J.O., Hendrickson, W.A. Description: Crystal Structure of the TorS sensor domain -TorT complex in the presence of T...
 
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'''Unreleased structure'''


The entry 3o1h is ON HOLD
==Crystal Structure of the TorS sensor domain - TorT complex in the presence of TMAO==
<StructureSection load='3o1h' size='340' side='right'caption='[[3o1h]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3o1h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O1H 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TMO:TRIMETHYLAMINE+OXIDE'>TMO</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=3o1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1h OCA], [https://pdbe.org/3o1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o1h RCSB], [https://www.ebi.ac.uk/pdbsum/3o1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q87ID1_VIBPA Q87ID1_VIBPA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The osmoregulator trimethylamine-N-oxide (TMAO), commonplace in aquatic organisms, is used as the terminal electron acceptor for respiration in many bacterial species. The TMAO reductase (Tor) pathway for respiratory catalysis is controlled by a receptor system that comprises the TMAO-binding protein TorT, the sensor histidine kinase TorS, and the response regulator TorR. Here we study the TorS/TorT sensor system to gain mechanistic insight into signaling by histidine kinase receptors. We determined crystal structures for complexes of TorS sensor domains with apo TorT and with TorT (TMAO); we characterized TorS sensor associations with TorT in solution; we analyzed the thermodynamics of TMAO binding to TorT-TorS complexes; and we analyzed in vivo responses to TMAO through the TorT/TorS/TorR system to test structure-inspired hypotheses. TorS-TorT(apo) is an asymmetric 2:2 complex that binds TMAO with negative cooperativity to form a symmetric active kinase.


Authors: Moore, J.O., Hendrickson, W.A.
An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO.,Moore JO, Hendrickson WA Structure. 2012 Apr 4;20(4):729-41. Epub 2012 Apr 3. PMID:22483119<ref>PMID:22483119</ref>


Description: Crystal Structure of the TorS sensor domain -TorT complex in the presence of TMAO
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:27:43 2010''
<div class="pdbe-citations 3o1h" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio parahaemolyticus]]
[[Category: Hendrickson WA]]
[[Category: Moore JO]]
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