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Two-component and phosphorelay signal transduction systems are central components in thevirulence and antimicrobial resistance responses of a number of bacterial and fungal pathogens;in somecases,these systems are essential for bacterial growth and viability.Herein,we analyze in detail the conservedsurface residue clusters in the phosphotransferase domain of histidine kinases and the regulatory domain ofresponse regulators by using complex structure-based three-dimensional cluster analysis.We also investigatethe protein-protein interactions that these residue clusters participate in.The Spo0B-Spo0F complex structurewas used as the reference structure,and the multiple aligned sequences of phosphotransferases and responseregulators were paired correspondingly.The results show that a contiguous conserved residue cluster isformed around the active site,which crosses the interface of histidine kinases and response regulators.Theconserved residue clusters of phosphotransferase and the regulatory domains are directly involved in thefunctional implementation of two-component signal transduction systems and are good targets for thedevelopment of novel antimicrobial agents.
Two-component and phosphorelay signal transduction systems are central components in the virulence and antimicrobial resistance responses of a number of bacterial and fungal pathogens; in somecases, these systems are essential for bacterial growth and viability. Herein, we analyze in detail the conserved surface residue clusters in the phosphotransferase domain of histidine kinases and the regulatory domain ofresponse regulators by using complex structure-based three-dimensional cluster analysis. We also investigate the protein-protein interactions that these residue clusters participate in. Spo0B-Spo0F complex structurewas used as the reference structure, and the multiple aligned sequences of phosphotransferases and responseregulators were paired correspondingly.The results show that a contiguous conserved residue cluster is formed around the active site, which crosses the interface of histidine kinases and response regulators .conserved residue clusters of phosphotransferase and the regula tory domains are directly involved in the functional implementation of two-component signal transduction systems and are good targets for the development of novel antimicrobial agents.