Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis.

ABSTRACT: Proteins are intrinsically flexible molecules. The role of internal motions in a protein's designated function is widely debated. The role of protein structure in enzyme catalysis is well established, and conservation of structural features provides vital clues to their role in function. Recently, it has been proposed that the protein function may involve multiple conformations: the observed deviations are not random thermodynamic fluctuations; rather, flexibility may be closely linked to protein function, including enzyme catalysis. We hypothesize that the argument of conservation of important structural features can also be extended to identification of protein flexibility in interconnection with enzyme function. Three classes of enzymes (prolyl-peptidyl isomerase, oxidoreductase, and nu

SUBMITTER: Ramanathan A 

PROVIDER: S-EPMC3210774 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature