Use of restrained molecular dynamics to predict the conformations of phosphorylated receiver domains in two-component signaling systems.

ABSTRACT: Two-component signaling (TCS) is the primary means by which bacteria, as well as certain plants and fungi, respond to external stimuli. Signal transduction involves stimulus-dependent autophosphorylation of a sensor histidine kinase and phosphoryl transfer to the receiver domain of a downstream response regulator. Phosphorylation acts as an allosteric switch, inducing structural and functional changes in the pathway's components. Due to their transient nature, phosphorylated receiver domains are challenging to characterize structurally. In this work, we provide a methodology for simulating receiver domain phosphorylation to predict conformations that are nearly identical to experimental structures. Using restrained molecular dynamics, phosphorylated conformations of receiver domains can be

SUBMITTER: Foster CA 

PROVIDER: S-EPMC5242315 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature