8h70
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8h70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H70 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8h70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H70 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.88Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=8h70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h70 OCA], [https://pdbe.org/8h70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h70 RCSB], [https://www.ebi.ac.uk/pdbsum/8h70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h70 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=8h70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h70 OCA], [https://pdbe.org/8h70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h70 RCSB], [https://www.ebi.ac.uk/pdbsum/8h70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h70 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/Q9KU10_VIBCH Q9KU10_VIBCH] Member of the two-component regulatory system PhoR/PhoB involved in the phosphate regulon genes expression. PhoR may function as a membrane-associated protein kinase that phosphorylates PhoB in response to environmental signals.[ARBA:ARBA00025207] |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | The two-component regulatory system (TCS) is a major regulatory system in bacteria that occurs in response to environmental changes and involves the sensor histidine kinase (HK) protein and response regulator (RR) protein. Among the TCSs, PhoR/PhoB is crucial for bacteria to adapt to changes in environmental phosphate concentrations. In addition, recent studies have shown that PhoR binding to the MgtC virulence factor activates phosphate transport for normal pathogenesis. In this work, we determined the crystal structure of the catalytic ATP binding domain of the PhoR sensor histidine kinase from Vibrio cholera, compared the structure with the known HK protein structures and discussed the potential binding interface with MgtC | + | The two-component regulatory system (TCS) is a major regulatory system in bacteria that occurs in response to environmental changes and involves the sensor histidine kinase (HK) protein and response regulator (RR) protein. Among the TCSs, PhoR/PhoB is crucial for bacteria to adapt to changes in environmental phosphate concentrations. In addition, recent studies have shown that PhoR binding to the MgtC virulence factor activates phosphate transport for normal pathogenesis. In this work, we determined the crystal structure of the catalytic ATP binding domain of the PhoR sensor histidine kinase from Vibrio cholera, compared the structure with the known HK protein structures and discussed the potential binding interface with MgtC. |
| - | Crystal structure of the catalytic ATP-binding domain of the PhoR sensor histidine kinase.,Jia R, Zhao Y, Hattori M Proteins. 2023 | + | Crystal structure of the catalytic ATP-binding domain of the PhoR sensor histidine kinase.,Jia R, Zhao Y, Hattori M Proteins. 2023 Jul;91(7):999-1004. doi: 10.1002/prot.26473. Epub 2023 Feb 17. PMID:36732678<ref>PMID:36732678</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Crystal structure of the catalytic ATP-binding domain of the PhoR sensor histidine kinase from Vibrio cholera
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