- EMDB-10050: Structure of the E. coli Chemotaxis Core Signaling Unit -
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基本情報
登録情報
データベース: EMDB / ID: EMD-10050
タイトル
Structure of the E. coli Chemotaxis Core Signaling Unit
マップデータ
E coli chemotaxis core signaling unit, cerrying receptor QQQQ mutations in the receptor.
試料
複合体: Bacterial chemotaxis core signaling complex
機能・相同性
機能・相同性情報
regulation of protein histidine kinase activity / negative regulation of protein modification process / detection of chemical stimulus / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / bacterial-type flagellum-dependent swimming motility / protein histidine kinase activity / protein trimerization / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis ...regulation of protein histidine kinase activity / negative regulation of protein modification process / detection of chemical stimulus / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / bacterial-type flagellum-dependent swimming motility / protein histidine kinase activity / protein trimerization / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / cell tip / regulation of chemotaxis / thermotaxis / signal complex assembly / receptor clustering / histidine kinase / phosphorelay signal transduction system / phosphorelay sensor kinase activity / establishment of localization in cell / cellular response to amino acid stimulus / cell motility / protein homooligomerization / chemotaxis / transmembrane signaling receptor activity / protein domain specific binding / signal transduction / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能
Biotechnology and Biological Sciences Research Council
BB/S003339/1
英国
引用
ジャーナル: Commun Biol / 年: 2020 タイトル: Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations. 著者: C Keith Cassidy / Benjamin A Himes / Dapeng Sun / Jun Ma / Gongpu Zhao / John S Parkinson / Phillip J Stansfeld / Zaida Luthey-Schulten / Peijun Zhang / 要旨: 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 ...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.