4KP4

Deciphering cis-trans directionality and visualizing autophosphorylation in histidine kinases.

4KP4 の概要

• エントリーDOI: 10.2210/pdb4kp4/pdb
• 分子名称: Osmolarity sensor protein EnvZ, Histidine kinase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: four helix-bundle, bergerat fold, kinase and phosphotransferase, atp binding, transferase-signaling protein complex, transferase/signaling protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P0AEJ4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52625.43

構造登録者

Casino, P.,Miguel-Romero, L.,Marina, A. (登録日: 2013-05-13, 公開日: 2014-02-12, 最終更新日: 2024-02-28)

主引用文献

Casino, P.,Miguel-Romero, L.,Marina, A.
Visualizing autophosphorylation in histidine kinases.
Nat Commun, 5:3258-3258, 2014

PubMed Abstract: Reversible protein phosphorylation is the most widespread regulatory mechanism in signal transduction. Autophosphorylation in a dimeric sensor histidine kinase is the first step in two-component signalling, the predominant signal-transduction device in bacteria. Despite being the most abundant sensor kinases in nature, the molecular bases of the histidine kinase autophosphorylation mechanism are still unknown. Furthermore, it has been demonstrated that autophosphorylation can occur in two directions, cis (intrasubunit) or trans (intersubunit) within the dimeric histidine kinase. Here, we present the crystal structure of the complete catalytic machinery of a chimeric histidine kinase. The structure shows an asymmetric histidine kinase dimer where one subunit is caught performing the autophosphorylation reaction. A structure-guided functional analysis on HK853 and EnvZ, two prototypical cis- and trans-phosphorylating histidine kinases, has allowed us to decipher the catalytic mechanism of histidine kinase autophosphorylation, which seems to be common independently of the reaction directionality.

PubMed: 24500224
DOI: 10.1038/ncomms4258

実験手法

X-RAY DIFFRACTION (3 Å)