Ligand-bound glutamine binding protein assumes multiple metastable binding sites with different binding affinities.

ABSTRACT: Protein dynamics plays key roles in ligand binding. However, the microscopic description of conformational dynamics-coupled ligand binding remains a challenge. In this study, we integrate molecular dynamics simulations, Markov state model (MSM) analysis and experimental methods to characterize the conformational dynamics of ligand-bound glutamine binding protein (GlnBP). We show that ligand-bound GlnBP has high conformational flexibility and additional metastable binding sites, presenting a more complex energy landscape than the scenario in the absence of ligand. The diverse conformations of GlnBP demonstrate different binding affinities and entail complex transition kinetics, implicating a concerted ligand binding mechanism. Single molecule fluorescence resonance energy transfer measureme

SUBMITTER: Zhang L 

PROVIDER: S-EPMC7400645 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature