Analysis of domain movements in glutamine-binding protein with simple models.

ABSTRACT: In this work, the mechanism of domain movements of glutamine-binding protein (GlnBP), especially the influence of the ligand on GlnBP dynamic behavior is investigated with the aid of a Gaussian network model (GNM) and an anisotropy elastic network model. The results show that the "open-closed" transition mainly appears as the large movement of the small domain, especially the top region including two alpha-helices and two beta-strands. The slowest mode of each three forms of GlnBP--ligand-free open, ligand-bound closed, and ligand-free closed GlnBP--shows that the open-closed motion of the two domains has a common hinge axis centered on Lys-87 and Gln-183. Accompanying the conformational transition, the residues within both large and small domains move in a highly coupled way. The peaks of

SUBMITTER: Su JG 

PROVIDER: S-EPMC1783873 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature