CryoEM and computer simulations reveal a novel kinase conformational switch in bacterial chemotaxis signaling.

ABSTRACT: 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 b

SUBMITTER: Cassidy CK 

PROVIDER: S-EPMC6746300 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature