3o1h
From Proteopedia
(Difference between revisions)
(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''' | ||
| - | + | ==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]] 3.10Å' 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]] 3.1Å</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. | ||
| - | + | 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 3o1h" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Vibrio parahaemolyticus]] | ||
| + | [[Category: Hendrickson WA]] | ||
| + | [[Category: Moore JO]] | ||
Current revision
Crystal Structure of the TorS sensor domain - TorT complex in the presence of TMAO
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