Conservation of flexible residue clusters among structural and functional enzyme homologues.

ABSTRACT: Conformational flexibility between structural ensembles is an essential component of enzyme function. Although the broad dynamical landscape of proteins is known to promote a number of functional events on multiple time scales, it is yet unknown whether structural and functional enzyme homologues rely on the same concerted residue motions to perform their catalytic function. It is hypothesized that networks of contiguous and flexible residue motions occurring on the biologically relevant millisecond time scale evolved to promote and/or preserve optimal enzyme catalysis. In this study, we use a combination of NMR relaxation dispersion, model-free analysis, and ligand titration experiments to successfully capture and compare the role of conformational flexibility between two structural homol

SUBMITTER: Gagne D 

PROVIDER: S-EPMC3531744 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature