Structural basis for ligand binding to an enzyme by a conformational selection pathway.

ABSTRACT: Proteins can bind target molecules through either induced fit or conformational selection pathways. In the conformational selection model, a protein samples a scarcely populated high-energy state that resembles a target-bound conformation. In enzymatic catalysis, such high-energy states have been identified as crucial entities for activity and the dynamic interconversion between ground states and high-energy states can constitute the rate-limiting step for catalytic turnover. The transient nature of these states has precluded direct observation of their properties. Here, we present a molecular description of a high-energy enzyme state in a conformational selection pathway by an experimental strategy centered on NMR spectroscopy, protein engineering, and X-ray crystallography. Through the i

SUBMITTER: Kovermann M 

PROVIDER: S-EPMC5474765 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature