3O1I

Crystal Structure of the TorS sensor domain - TorT complex in the absence of ligand

3O1I の概要

• エントリーDOI: 10.2210/pdb3o1i/pdb
• 関連するPDBエントリー: 3I9W 3I9Y 3O1H 3O1J
• 分子名称: Sensor protein TorS, Periplasmic protein TorT, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL, ... (4 entities in total)
• 機能のキーワード: ligand free, two component sensor, periplasmic binding protein, tmao, signaling protein
• 由来する生物種: Vibrio parahaemolyticus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 131532.53

構造登録者

Moore, J.O.,Hendrickson, W.A. (登録日: 2010-07-21, 公開日: 2011-12-21, 最終更新日: 2024-11-06)

主引用文献

Moore, J.O.,Hendrickson, W.A.
An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO.
Structure, 20:729-741, 2012

PubMed Abstract: The osmoregulator trimethylamine-N-oxide (TMAO), commonplace in aquatic organisms, is used as the terminal electron acceptor for respiration in many bacterial species. The TMAO reductase (Tor) pathway for respiratory catalysis is controlled by a receptor system that comprises the TMAO-binding protein TorT, the sensor histidine kinase TorS, and the response regulator TorR. Here we study the TorS/TorT sensor system to gain mechanistic insight into signaling by histidine kinase receptors. We determined crystal structures for complexes of TorS sensor domains with apo TorT and with TorT (TMAO); we characterized TorS sensor associations with TorT in solution; we analyzed the thermodynamics of TMAO binding to TorT-TorS complexes; and we analyzed in vivo responses to TMAO through the TorT/TorS/TorR system to test structure-inspired hypotheses. TorS-TorT(apo) is an asymmetric 2:2 complex that binds TMAO with negative cooperativity to form a symmetric active kinase.

PubMed: 22483119
DOI: 10.1016/j.str.2012.02.021

実験手法

X-RAY DIFFRACTION (2.8 Å)