Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism.

ABSTRACT: Large-scale conformational changes in proteins are often associated with the binding of a substrate. Because conformational changes may be related to the function of an enzyme, understanding the kinetics and energetics of these motions is very important. We have delineated the atomically detailed conformational transition pathway of the phosphotransferase enzyme adenylate kinase (AdK) in the absence and presence of an inhibitor. The computed free energy profiles associated with conformational transitions offer detailed mechanistic insights into, as well as kinetic information on, the ligand binding mechanism. Specifically, potential of mean force calculations reveal that in the ligand-free state, there is no significant barrier separating the open and closed conformations of AdK. The enzym

SUBMITTER: Arora K 

PROVIDER: S-EPMC2141805 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature