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-Structure paper
タイトル | CryoEM and computer simulations reveal a novel kinase conformational switch in bacterial chemotaxis signaling. |
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ジャーナル・号・ページ | Elife, Vol. 4, Year 2015 |
掲載日 | 2015年11月19日 |
著者 | C Keith Cassidy / Benjamin A Himes / Frances J Alvarez / Jun Ma / Gongpu Zhao / Juan R Perilla / Klaus Schulten / Peijun Zhang / |
PubMed 要旨 | Chemotactic responses in bacteria require large, highly ordered arrays of sensory proteins to mediate the signal transduction that ultimately controls cell motility. A mechanistic understanding of ...Chemotactic responses in bacteria require large, highly ordered arrays of sensory proteins to mediate the signal transduction that ultimately controls cell motility. A mechanistic understanding of the molecular events underlying signaling, however, has been hampered by the lack of a high-resolution structural description of the extended array. Here, we report a novel reconstitution of the array, involving the receptor signaling domain, histidine kinase CheA, and adaptor protein CheW, as well as a density map of the core-signaling unit at 11.3 Å resolution, obtained by cryo-electron tomography and sub-tomogram averaging. Extracting key structural constraints from our density map, we computationally construct and refine an atomic model of the core array structure, exposing novel interfaces between the component proteins. Using all-atom molecular dynamics simulations, we further reveal a distinctive conformational change in CheA. Mutagenesis and chemical cross-linking experiments confirm the importance of the conformational dynamics of CheA for chemotactic function. |
リンク | Elife / PubMed:26583751 / PubMed Central |
手法 | EM (トモグラフィー) / EM (サブトモグラム平均) |
解像度 | 11.3 - 17.5 Å |
構造データ | EMDB-3234: EMDB-6319: Structure of bacterial chemotaxis signaling CheA2-trimer core complex by cryo-electron tomography and subvolume averaging EMDB-6320: |
由来 |
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キーワード | SIGNALING PROTEIN / bacterial chemotaxis / core-signaling unit / adaptor protein / histidine kinase / chemoreceptor |