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

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.

Hidden diversity and potential ecological function of phosphorus acquisition genes in widespread terrestrial bacteriophages

“…All protein sequences of the ppa and phoR genes had complete conserved active residues (Supplementary Figs. 1 – 3 ): PPa (including Family I and Family II), Asp residues coordinating Mg 2+ /Mn 2+ (DxdxxD or DHH) 26 ; PhoR, ATP binding (NxxxNaxky, Dxgxgi, gLa, F) 27 . The majority of protein sequences of the phoD (19/23) and pstS genes (4/6) had completely conserved active residues (Supplementary Figs.…”