Simulated pressure changes in LacI suggest a link between hydration and functional conformational changes.

ABSTRACT: The functions of many proteins are associated with interconversions among conformational substates. However, these substates can be difficult to measure experimentally, and determining contributions from hydration changes can be especially difficult. Here, we assessed the use of pressure perturbations to sample the substates accessible to the Escherichia coli lactose repressor protein (LacI) in various liganded forms. In the presence of DNA, the regulatory domain of LacI adopts an Open conformation that, in the absence of DNA, changes to a Closed conformation. Increasing the simulation pressure prevented the transition from an Open to a Closed conformation, in a similar manner to the binding of DNA and anti-inducer, ONPF. The results suggest the hydration of specific residues play a signif

SUBMITTER: Kariyawasam NL 

PROVIDER: S-EPMC10842697 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature