5UHT

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

5UHT の概要

• エントリーDOI: 10.2210/pdb5uht/pdb
• 分子名称: Sensor histidine kinase, Response regulator, ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• 機能のキーワード: two component system hk853 rr468, transferase-signaling protein complex, transferase/signaling protein
• 由来する生物種: Thermotoga maritima; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88865.51

構造登録者

Liu, Y.,Rose, J.,Jiang, L.,Zhou, P. (登録日: 2017-01-12, 公開日: 2017-12-27, 最終更新日: 2024-11-06)

主引用文献

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

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: 29235472
DOI: 10.1038/s41467-017-02310-9

実験手法

X-RAY DIFFRACTION (2.68 Å)