6rh7 | pdb_00006rh7

Revisiting pH-gated conformational switch. Complex HK853 mutant H260A -RR468 mutant D53A pH 7.5

spinqualitylabelsall models 6rh7, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rh7 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases.,Mideros-Mora C, Miguel-Romero L, Felipe-Ruiz A, Casino P, Marina A Nat Commun. 2020 Feb 7;11(1):769. doi: 10.1038/s41467-020-14540-5. PMID:32034139 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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