3o1j: Difference between revisions
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== | ==Crystal Structure of the TorS sensor domain - TorT complex in the absence of isopropanol== | ||
[[3o1j]] is a 4 chain structure with sequence from [ | <StructureSection load='3o1j' size='340' side='right'caption='[[3o1j]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
[[Category: | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3o1j]] is a 4 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=3O1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O1J 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]] 2.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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=3o1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1j OCA], [https://pdbe.org/3o1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o1j RCSB], [https://www.ebi.ac.uk/pdbsum/3o1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1j 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3o1j" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Vibrio parahaemolyticus]] | [[Category: Vibrio parahaemolyticus]] | ||
[[Category: Hendrickson | [[Category: Hendrickson WA]] | ||
[[Category: Moore | [[Category: Moore JO]] | ||