3a0t: Difference between revisions

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<StructureSection load='3a0t' size='340' side='right'caption='[[3a0t]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
<StructureSection load='3a0t' size='340' side='right'caption='[[3a0t]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3a0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A0T FirstGlance]. <br>
<table><tr><td colspan='2'>[[3a0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A0T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a0r|3a0r]], [[3a0s|3a0s]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_1359 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></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=3a0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a0t OCA], [https://pdbe.org/3a0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a0t RCSB], [https://www.ebi.ac.uk/pdbsum/3a0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a0t ProSAT]</span></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=3a0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a0t OCA], [https://pdbe.org/3a0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a0t RCSB], [https://www.ebi.ac.uk/pdbsum/3a0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a0t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9X180_THEMA Q9X180_THEMA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a0t ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a0t ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We determined the structure of the complex of the sensory histidine kinase (HK) and its cognate response regulator (RR) in the two-component signal transduction system of Thermotoga maritima. This was accomplished by fitting the high-resolution structures of the isolated HK domains and the RR onto the electron density map (3.8 A resolution) of the HK/RR complex crystal. Based on the structural information, we evaluated the roles of both interdomain and intermolecular interactions in the signal transduction of the cytosolic PAS-linked HK and RR system, in particular the O(2)-sensor FixL/FixJ system. The PAS-sensor domain of HK interacts with the catalytic domain of the same polypeptide chain by creating an interdomain beta sheet. The interaction site between HK and RR, which was confirmed by NMR, is suitable for the intermolecular transfer reaction of the phosphoryl group, indicating that the observed interaction is important for the phosphatase activity of HK that dephosphorylates phospho-RR.
Structure of PAS-linked histidine kinase and the response regulator complex.,Yamada S, Sugimoto H, Kobayashi M, Ohno A, Nakamura H, Shiro Y Structure. 2009 Oct 14;17(10):1333-44. PMID:19836334<ref>PMID:19836334</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3a0t" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Histidine kinase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kobayashi, M]]
[[Category: Thermotoga maritima]]
[[Category: Nakamura, H]]
[[Category: Kobayashi M]]
[[Category: Ohno, A]]
[[Category: Nakamura H]]
[[Category: Shiro, Y]]
[[Category: Ohno A]]
[[Category: Sugimoto, H]]
[[Category: Shiro Y]]
[[Category: Yamada, S]]
[[Category: Sugimoto H]]
[[Category: Atp-lid]]
[[Category: Yamada S]]
[[Category: Kinase]]
[[Category: Phosphoprotein]]
[[Category: Transferase]]
[[Category: Two-component regulatory system]]

Latest revision as of 13:59, 13 March 2024

Catalytic domain of histidine kinase ThkA (TM1359) in complex with ADP and Mg ion (trigonal)

3a0t, resolution 1.91Å

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