3a0y: Difference between revisions
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==Catalytic domain of histidine kinase ThkA (TM1359) (nucleotide free form 3: 1,2-propanediol, orthorombic)== | ==Catalytic domain of histidine kinase ThkA (TM1359) (nucleotide free form 3: 1,2-propanediol, orthorombic)== | ||
<StructureSection load='3a0y' size='340' side='right' caption='[[3a0y]], [[Resolution|resolution]] 1.57Å' scene=''> | <StructureSection load='3a0y' size='340' side='right'caption='[[3a0y]], [[Resolution|resolution]] 1.57Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3a0y]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3a0y]] is a 2 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=3A0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A0Y FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a0t|3a0t]], [[3a0s|3a0s]], [[3a0u|3a0u]], [[3a0r|3a0r]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a0t|3a0t]], [[3a0s|3a0s]], [[3a0u|3a0u]], [[3a0r|3a0r]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_1359 ([ | <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'>[ | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3a0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a0y OCA], [https://pdbe.org/3a0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a0y RCSB], [https://www.ebi.ac.uk/pdbsum/3a0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a0y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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[[Category: Atcc 43589]] | [[Category: Atcc 43589]] | ||
[[Category: Histidine kinase]] | [[Category: Histidine kinase]] | ||
[[Category: Large Structures]] | |||
[[Category: Kobayashi, M]] | [[Category: Kobayashi, M]] | ||
[[Category: Nakamura, H]] | [[Category: Nakamura, H]] | ||
Revision as of 19:13, 22 December 2021
Catalytic domain of histidine kinase ThkA (TM1359) (nucleotide free form 3: 1,2-propanediol, orthorombic)Catalytic domain of histidine kinase ThkA (TM1359) (nucleotide free form 3: 1,2-propanediol, orthorombic)
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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