6AZR
Crystal structure of the T264A HK853cp-BeF3-RR468 complex
Summary for 6AZR
| Entry DOI | 10.2210/pdb6azr/pdb |
| Descriptor | Sensor histidine kinase, Chemotaxis regulator-transmits chemoreceptor signals to flagelllar motor components CheY, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | kinase, phosphatase, response regulator, two-component system, signaling protein |
| Biological source | Thermotoga maritima More |
| Total number of polymer chains | 4 |
| Total formula weight | 88108.80 |
| Authors | |
| Primary citation | Liu, Y.,Rose, J.,Huang, S.,Hu, Y.,Wu, Q.,Wang, D.,Li, C.,Liu, M.,Zhou, P.,Jiang, L. A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases. Nat Commun, 8:2104-2104, 2017 Cited by PubMed Abstract: 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. PubMed: 29235472DOI: 10.1038/s41467-017-02310-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.628 Å) |
Structure validation
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