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| <StructureSection load='6azr' size='340' side='right'caption='[[6azr]], [[Resolution|resolution]] 3.63Å' scene=''> | | <StructureSection load='6azr' size='340' side='right'caption='[[6azr]], [[Resolution|resolution]] 3.63Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6azr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AZR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AZR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6azr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AZR FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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]] 3.628Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</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_0853 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), Tmari_0465 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=6azr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6azr OCA], [https://pdbe.org/6azr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6azr RCSB], [https://www.ebi.ac.uk/pdbsum/6azr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6azr ProSAT]</span></td></tr> |
- | <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=6azr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6azr OCA], [http://pdbe.org/6azr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6azr RCSB], [http://www.ebi.ac.uk/pdbsum/6azr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6azr ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q9WZV7_THEMA Q9WZV7_THEMA] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Thema]] | + | [[Category: Thermotoga maritima MSB8]] |
- | [[Category: Rose, J]] | + | [[Category: Rose J]] |
- | [[Category: Zhou, P]] | + | [[Category: Zhou P]] |
- | [[Category: Kinase]]
| + | |
- | [[Category: Phosphatase]]
| + | |
- | [[Category: Response regulator]]
| + | |
- | [[Category: Signaling protein]]
| + | |
- | [[Category: Two-component system]]
| + | |
| Structural highlights
Function
Q9WZV7_THEMA
Publication Abstract from PubMed
Histidine kinases are key regulators in the bacterial two-component systems that mediate the cellular response to environmental changes. The vast majority of the sensor histidine kinases belong to the bifunctional HisKA family, displaying both kinase and phosphatase activities toward their substrates. The molecular mechanisms regulating the opposing activities of these enzymes are not well understood. Through a combined NMR and crystallographic study on the histidine kinase HK853 and its response regulator RR468 from Thermotoga maritima, here we report a pH-mediated conformational switch of HK853 that shuts off its phosphatase activity under acidic conditions. Such a pH-sensing mechanism is further demonstrated in the EnvZ-OmpR two-component system from Salmonella enterica in vitro and in vivo, which directly contributes to the bacterial infectivity. Our finding reveals a broadly conserved mechanism that regulates the phosphatase activity of the largest family of bifunctional histidine kinases in response to the change of environmental pH.
A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.,Liu Y, Rose J, Huang S, Hu Y, Wu Q, Wang D, Li C, Liu M, Zhou P, Jiang L Nat Commun. 2017 Dec 13;8(1):2104. doi: 10.1038/s41467-017-02310-9. PMID:29235472[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu Y, Rose J, Huang S, Hu Y, Wu Q, Wang D, Li C, Liu M, Zhou P, Jiang L. A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases. Nat Commun. 2017 Dec 13;8(1):2104. doi: 10.1038/s41467-017-02310-9. PMID:29235472 doi:http://dx.doi.org/10.1038/s41467-017-02310-9
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