8h70

Crystal structure of the catalytic ATP-binding domain of the PhoR sensor histidine kinase from Vibrio cholera

spinqualitylabelsall models 8h70, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8h70 is a 1 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.88Å Ligands: PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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] 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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