5uht | pdb_00005uht

Structure of the Thermotoga maritima HK853-BeF3-RR468 complex at pH 5.0

spinqualitylabelsall models 5uht, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5uht is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, GOL, MG, SO4 NonStd Res: BFD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Histidine kinases are key regulators in the bacterial two-component systems that mediate the cellular response to environmental changes. The vast majority of the sensor histidine kinases belong to the bifunctional HisKA family, displaying both kinase and phosphatase activities toward their substrates. The molecular mechanisms regulating the opposing activities of these enzymes are not well understood. Through a combined NMR and crystallographic study on the histidine kinase HK853 and its response regulator RR468 from Thermotoga maritima, here we report a pH-mediated conformational switch of HK853 that shuts off its phosphatase activity under acidic conditions. Such a pH-sensing mechanism is further demonstrated in the EnvZ-OmpR two-component system from Salmonella enterica in vitro and in vivo, which directly contributes to the bacterial infectivity. Our finding reveals a broadly conserved mechanism that regulates the phosphatase activity of the largest family of bifunctional histidine kinases in response to the change of environmental pH. A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.,Liu Y, Rose J, Huang S, Hu Y, Wu Q, Wang D, Li C, Liu M, Zhou P, Jiang L Nat Commun. 2017 Dec 13;8(1):2104. doi: 10.1038/s41467-017-02310-9. PMID:29235472 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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