Guanylate kinase, induced fit, and the allosteric spring probe.

ABSTRACT: Since the introduction of the induced-fit theory by D. E. Koshland Jr., it has been established that conformational motion invariably accompanies the execution of protein function. The catalytic activity of kinases, specifically, is associated with large conformational changes ( approximately 1 nm amplitude). In the case of guanylate kinase, upon substrate binding, the LID and nucleotide-monophosphate-binding domains are brought together and toward the CORE with large concerted movements about the alpha3 (helix 3) axis. However, whether the change in conformation mostly affects the catalytic rate or mostly increases binding affinities for one or the other substrate is unclear. We investigate this question using a nanotechnology approach based on mechanical stress. Using an "allosteric spri

SUBMITTER: Choi B 

PROVIDER: S-EPMC1796832 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature