3I9W

Crystal structure of the E. coli histidine kinase sensor TorS sensor domain

3I9W の概要

• エントリーDOI: 10.2210/pdb3i9w/pdb
• 分子名称: Sensor protein torS (2 entities in total)
• 機能のキーワード: stacked two four-helix bundles, atp-binding, cell inner membrane, cell membrane, kinase, membrane, nucleotide-binding, phosphoprotein, transferase, transmembrane, two-component regulatory system
• 由来する生物種: Escherichia coli K-12
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : P39453
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32449.15

構造登録者

Moore, J.O.,Hendrickson, W.A. (登録日: 2009-07-13, 公開日: 2009-10-06, 最終更新日: 2024-02-21)

主引用文献

Moore, J.O.,Hendrickson, W.A.
Structural analysis of sensor domains from the TMAO-responsive histidine kinase receptor TorS
Structure, 17:1195-1204, 2009

PubMed Abstract: Histidine kinase receptors respond to diverse signals and mediate signal transduction across the plasma membrane in all prokaryotes and certain eukaryotes. Each receptor is part of a two-component system that regulates a particular cellular process. Organisms that use trimethylamine-N-oxide (TMAO) as a terminal electron acceptor typically control their anaerobic respiration through the TMAO reductase (Tor) pathway, which the TorS histidine kinase activates when sensing TMAO in the environment. We have determined crystal structures for the periplasmic sensor domains of TorS receptors from Escherichia coli and Vibrio parahaemolyticus. TorS sensor domains have a novel fold consisting of a membrane-proximal right-handed four-helical bundle and a membrane-distal left-handed four-helical bundle, but conformational dispositions differ significantly in the two structures. Isolated TorS sensor domains dimerize in solution; and from comparisons with dimeric NarX and Tar sensors, we postulate that signaling through TorS dimers involves a piston-type displacement between helices.

PubMed: 19748340
DOI: 10.1016/j.str.2009.07.015

実験手法

X-RAY DIFFRACTION (2.7 Å)