3EZH

Crystal Structure of the E. coli Histidine Kinase NarX Sensor Domain in Complex with Nitrate

3EZH の概要

• エントリーDOI: 10.2210/pdb3ezh/pdb
• 関連するPDBエントリー: 3EZI
• 分子名称: Nitrate/nitrite sensor protein narX, NITRATE ION (3 entities in total)
• 機能のキーワード: histidine kinase, sensor domain, sensor protein, four-helix bundle, nitrate sensor, selenomethionyl mad, signal transduction, cell inner membrane, cell membrane, kinase, membrane, nitrate assimilation, phosphoprotein, transferase, transmembrane, two-component regulatory system
• 由来する生物種: Escherichia coli K12
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : P0AFA2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28362.47

構造登録者

Cheung, J.,Hendrickson, W.A. (登録日: 2008-10-22, 公開日: 2008-12-23, 最終更新日: 2024-11-20)

主引用文献

Cheung, J.,Hendrickson, W.A.
Structural Analysis of Ligand Stimulation of the Histidine Kinase NarX.
Structure, 17:190-201, 2009

PubMed Abstract: Histidine kinase receptors are a large family of membrane-spanning proteins found in many prokaryotes and some eukaryotes. They are a part of two-component signal transduction systems, which each comprise a sensor kinase and a response regulator and are involved with the regulation of many cellular processes. NarX is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria. We present high-resolution X-ray crystal structures of the periplasmic sensor domain from Escherichia coli NarX in a complex with nitrate and in the apo state. Our analysis reveals that nitrate-binding induces conformation changes that result in a piston-type displacement between the N- and C-terminal helices of the periplasmic domain. Such conformational changes might represent a conserved mechanism of signaling in histidine kinases by which ligand binding is communicated across the lipid bilayer.

PubMed: 19217390
DOI: 10.1016/j.str.2008.12.013

実験手法

X-RAY DIFFRACTION (1.7 Å)