3DGF

Structure of a histidine kinase-response regulator complex reveals insights into Two-component signaling and a novel cis-autophosphorylation mechanism

3DGF の概要

• エントリーDOI: 10.2210/pdb3dgf/pdb
• 関連するPDBエントリー: 3DGE
• 分子名称: Response regulator (2 entities in total)
• 機能のキーワード: receiver domain, signaling protein
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13848.26

構造登録者

Casino, P.,Marina, A. (登録日: 2008-06-13, 公開日: 2009-07-07, 最終更新日: 2024-04-03)

主引用文献

Casino, P.,Rubio, V.,Marina, A.
Structural Insight into Partner Specificity and Phosphoryl Transfer in Two-Component Signal Transduction.
Cell(Cambridge,Mass.), 139:1-12, 2009

PubMed Abstract: The chief mechanism used by bacteria for sensing their environment is based on two conserved proteins: a sensor histidine kinase (HK) and an effector response regulator (RR). The signal transduction process involves highly conserved domains of both proteins that mediate autokinase, phosphotransfer, and phosphatase activities whose output is a finely tuned RR phosphorylation level. Here, we report the structure of the complex between the entire cytoplasmic portion of Thermotoga maritima class I HK853 and its cognate, RR468, as well as the structure of the isolated RR468, both free and BeF(3)(-) bound. Our results provide insight into partner specificity in two-component systems, recognition of the phosphorylation state of each partner, and the catalytic mechanism of the phosphatase reaction. Biochemical analysis shows that the HK853-catalyzed autokinase reaction proceeds by a cis autophosphorylation mechanism within the HK subunit. The results suggest a model for the signal transduction mechanism in two-component systems.

PubMed: 19800110
DOI: 10.1016/j.cell.2009.08.032

実験手法

X-RAY DIFFRACTION (2 Å)