8H70

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

Summary for 8H70

• Entry DOI: 10.2210/pdb8h70/pdb
• Descriptor: Phosphate regulon sensor protein PhoR, DI(HYDROXYETHYL)ETHER (3 entities in total)
• Functional Keywords: histidine kinase, membrane protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 1
• Total formula weight: 18332.92

Authors

Jia, R.,Zhao, W.,Hattori, M. (deposition date: 2022-10-18, release date: 2023-02-15, Last modification date: 2024-05-29)

Primary citation

Jia, R.,Zhao, Y.,Hattori, M.
Crystal structure of the catalytic ATP-binding domain of the PhoR sensor histidine kinase.
Proteins, 91:999-1004, 2023

PubMed Abstract: 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.

PubMed: 36732678
DOI: 10.1002/prot.26473

Experimental method

X-RAY DIFFRACTION (1.88 Å)