Control of catalytic efficiency by a coevolving network of catalytic and noncatalytic residues.

ABSTRACT: The active sites of enzymes consist of residues necessary for catalysis and structurally important noncatalytic residues that together maintain the architecture and function of the active site. Examples of evolutionary interactions between catalytic and noncatalytic residues have been difficult to define and experimentally validate due to a general intolerance of these residues to substitution. Here, using computational methods to predict coevolving residues, we identify a network of positions consisting of two catalytic metal-binding residues and two adjacent noncatalytic residues in LAGLIDADG homing endonucleases (LHEs). Distinct combinations of the four residues in the network map to distinct LHE subfamilies, with a striking distribution of the metal-binding Asp (D) and Glu (E) residues

SUBMITTER: McMurrough TA 

PROVIDER: S-EPMC4060692 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature