Allosteric Priming of E. coli CheY by the Flagellar Motor Protein FliM.

ABSTRACT: Phosphorylation of Escherichia coli CheY protein transduces chemoreceptor stimulation to a highly cooperative flagellar motor response. CheY binds to the N-terminal peptide of the FliM motor protein (FliM_N). Constitutively active D13K-Y106W CheY has been an important tool for motor physiology. The crystal structures of CheY and CheY ⋅ FliM_N with and without D13K-Y106W have shown FliM_N-bound CheY contains features of both active and inactive states. We used molecular dynamics (MD) simulations to characterize the CheY conformational landscape accessed by FliM_N and D13K-Y106W. Mutual information measures identified the central features of the long-range CheY allosteric network between D57 phosphorylation site and the FliM_N interface, name

SUBMITTER: Wheatley P 

PROVIDER: S-EPMC7499101 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature