4CB0

Crystal structure of CpxAHDC in complex with ATP (hexagonal form)

4CB0 の概要

• エントリーDOI: 10.2210/pdb4cb0/pdb
• 関連するPDBエントリー: 4BIU 4BIV 4BIW 4BIX 4BIY 4BIZ
• 分子名称: SENSOR PROTEIN CPXA, ADENOSINE-5'-TRIPHOSPHATE, SULFATE ION (3 entities in total)
• 機能のキーワード: transferase, signal transduction, two-components systems, histidine kinases
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : P0AE82
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68937.97

構造登録者

Mechaly, A.E.,Sassoon, N.,Betton, J.M.,Alzari, P.M. (登録日: 2013-10-09, 公開日: 2014-02-12, 最終更新日: 2017-07-12)

主引用文献

Mechaly, A.E.,Sassoon, N.,Betton, J.M.,Alzari, P.M.
Segmental Helical Motions and Dynamical Asymmetry Modulate Histidine Kinase Autophosphorylation.
Plos Biol., 12:1776-, 2014

PubMed Abstract: Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP domain to control the transient interaction between the histidine-containing and ATP-binding domains during the catalytic reaction. Here we report crystal structures of the full cytoplasmic region of CpxA, a prototypical HK involved in Escherichia coli response to envelope stress. The structural ensemble, which includes the Michaelis complex, unveils HK activation as a highly dynamic process, in which HAMP modulates the segmental mobility of the central HK α-helices to promote a strong conformational and dynamical asymmetry that characterizes the kinase-active state. A mechanical model based on our structural and biochemical data provides insights into HAMP-mediated signal transduction, the autophosphorylation reaction mechanism, and the symmetry-dependent control of HK kinase/phosphatase functional states.

PubMed: 24492262
DOI: 10.1371/JOURNAL.PBIO.1001776

実験手法

X-RAY DIFFRACTION (3.3 Å)