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3o1h

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==Crystal Structure of the TorS sensor domain - TorT complex in the presence of TMAO==
==Crystal Structure of the TorS sensor domain - TorT complex in the presence of TMAO==
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<StructureSection load='3o1h' size='340' side='right' caption='[[3o1h]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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<StructureSection load='3o1h' size='340' side='right'caption='[[3o1h]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o1h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O1H FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TMO:TRIMETHYLAMINE+OXIDE'>TMO</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]] 3.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i9y|3i9y]], [[3i9w|3i9w]], [[3o1i|3o1i]], [[3o1j|3o1j]]</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=TMO:TRIMETHYLAMINE+OXIDE'>TMO</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TorS, VPA0675 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=670 "Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961]), TorT, VPA0674 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=670 "Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961])</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=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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></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=3o1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1h OCA], [http://pdbe.org/3o1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o1h RCSB], [http://www.ebi.ac.uk/pdbsum/3o1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1h ProSAT]</span></td></tr>
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</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/Q87ID1_VIBPA Q87ID1_VIBPA]
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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.
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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>
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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 3o1h" 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: Histidine kinase]]
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[[Category: Large Structures]]
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[[Category: Hendrickson, W A]]
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[[Category: Vibrio parahaemolyticus]]
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[[Category: Moore, J O]]
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[[Category: Hendrickson WA]]
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[[Category: Periplasmic binding protein]]
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[[Category: Moore JO]]
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[[Category: Signaling protein]]
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[[Category: Tmao binding]]
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[[Category: Tmao bound]]
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[[Category: Two component sensor]]
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Current revision

Crystal Structure of the TorS sensor domain - TorT complex in the presence of TMAO

PDB ID 3o1h

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