Crystal structure of the catalytic ATP‐binding domain of the PhoR sensor histidine kinase

Author:

Jia Ruiliang1,Zhao Yimeng12,Hattori Motoyuki1

Affiliation:

1. State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Shanghai Key Laboratory of Bioactive Small Molecules, Department of Physiology and Neurobiology School of Life Sciences, Fudan University Shanghai China

2. Human Phenome Institute Fudan University Shanghai China

Abstract

AbstractThe 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.

Funder

National Natural Science Foundation of China

Shanghai Municipal Education Commission

State Key Laboratory of Genetic Engineering

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

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