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Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
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Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
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Journal Article
Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
2020
Overview
Histidine is a versatile residue playing key roles in enzyme catalysis thanks to the chemistry of its imidazole group that can serve as nucleophile, general acid or base depending on its protonation state. In bacteria, signal transduction relies on two-component systems (TCS) which comprise a sensor histidine kinase (HK) containing a phosphorylatable catalytic His with phosphotransfer and phosphatase activities over an effector response regulator. Recently, a pH-gated model has been postulated to regulate the phosphatase activity of HisKA HKs based on the pH-dependent rotamer switch of the phosphorylatable His. Here, we have revisited this model from a structural and functional perspective on HK853–RR468 and EnvZ–OmpR TCS, the prototypical HisKA HKs. We have found that the rotamer of His is not influenced by the environmental pH, ruling out a pH-gated model and confirming that the chemistry of the His is responsible for the decrease in the phosphatase activity at acidic pH.
Bacterial two-component systems are composed of a sensor histidine kinase (HK) and an effector response regulator and upon signal detection, the HK autophosphorylates a conserved His residue. Here the authors structurally and functionally characterise two HKs, HK853–RR468 and EnvZ–OmpR, and find that the rotamer of the phosphorylatable catalytic His is not influenced by the environmental pH, ruling out an earlier proposed pH-gated model.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/45
/ 82/83
/ 96
/ 96/95
/ Bacterial Outer Membrane Proteins - chemistry
/ Bacterial Outer Membrane Proteins - metabolism
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - metabolism
/ Histidine Kinase - chemistry
/ Histidine Kinase - metabolism
/ Humanities and Social Sciences
/ Kinases
/ Multienzyme Complexes - chemistry
/ Multienzyme Complexes - metabolism
/ Mutation
/ Science
/ Structure-function relationships
/ Thermotoga maritima - enzymology
/ Thermotoga maritima - genetics
