Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme.

ABSTRACT: Several enzymes are known to have evolved from non-catalytic proteins such as solute-binding proteins (SBPs). Although attention has been focused on how a binding site can evolve to become catalytic, an equally important question is: how do the structural dynamics of a binding protein change as it becomes an efficient enzyme? Here we performed a variety of experiments, including propargyl-DO3A-Gd(III) tagging and double electron-electron resonance (DEER) to study the rigid body protein dynamics of reconstructed evolutionary intermediates to determine how the conformational sampling of a protein changes along an evolutionary trajectory linking an arginine SBP to a cyclohexadienyl dehydratase (CDT). We observed that primitive dehydratases predominantly populate catalytically unproductive con

SUBMITTER: Kaczmarski JA 

PROVIDER: S-EPMC7683729 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature