Dynamics of firefly luciferase inhibition by general anesthetics: Gaussian and anisotropic network analyses.

ABSTRACT: The new crystal structures of the product-bound firefly luciferase combined with the previously determined substrate-free structures allow for a detailed analysis of the dynamics basis for the luciferase enzymatic activities. Using the Gaussian network model and the anisotropic network model, we show here that the superposition of the three slowest anisotropic network model modes, consisting of the bending, rotating, and rocking motions of the C-domain, accounts for large rearrangement of domains from the substrate-free (open) to product-bound (closed) conformation and thus constitutes a critical component of the enzyme's functions. The analysis also offers a unique platform to reexamine the molecular mechanism of the anesthetic inhibition of the firefly luciferase. Through perturbing the

SUBMITTER: Szarecka A 

PROVIDER: S-EPMC1959537 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature