6S1K

E. coli Core Signaling Unit, carrying QQQQ receptor mutation

6S1K の概要

• エントリーDOI: 10.2210/pdb6s1k/pdb
• EMDBエントリー: 10050
• 分子名称: Chemotaxis protein CheA, CheW, Methyl-accepting chemotaxis protein I (3 entities in total)
• 機能のキーワード: chemotaxis, methyl-accepting chemotaxis protein, histidine kinase, signaling protein
• 由来する生物種: Escherichia coli str. K-12 substr. MG1655star; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 893048.84

構造登録者

Cassidy, C.K. (登録日: 2019-06-18, 公開日: 2020-01-22, 最終更新日: 2024-05-15)

主引用文献

Cassidy, C.K.,Himes, B.A.,Sun, D.,Ma, J.,Zhao, G.,Parkinson, J.S.,Stansfeld, P.J.,Luthey-Schulten, Z.,Zhang, P.
Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations.
Commun Biol, 3:24-24, 2020

PubMed Abstract: To enable the processing of chemical gradients, chemotactic bacteria possess large arrays of transmembrane chemoreceptors, the histidine kinase CheA, and the adaptor protein CheW, organized as coupled core-signaling units (CSU). Despite decades of study, important questions surrounding the molecular mechanisms of sensory signal transduction remain unresolved, owing especially to the lack of a high-resolution CSU structure. Here, we use cryo-electron tomography and sub-tomogram averaging to determine a structure of the Escherichia coli CSU at sub-nanometer resolution. Based on our experimental data, we use molecular simulations to construct an atomistic model of the CSU, enabling a detailed characterization of CheA conformational dynamics in its native structural context. We identify multiple, distinct conformations of the critical P4 domain as well as asymmetries in the localization of the P3 bundle, offering several novel insights into the CheA signaling mechanism.

PubMed: 31925330
DOI: 10.1038/s42003-019-0748-0

実験手法

ELECTRON MICROSCOPY (8.38 Å)