Quaternary Structure Analyses of an Essential Oligomeric Enzyme

Abstract

Here, we review recent studies aimed at defining the importance of quaternary structure to a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate the complementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugation with enzyme kinetics, in vitro mutagenesis, macromolecular crystallography, small angle X-ray scattering, and molecular dynamics simulations, to demonstrate the role of subunit self-association in facilitating protein dynamics and enzyme function. This multitechnique approach has yielded new insights into the molecular evolution of protein quaternary structure.

Keywords: Analytical ultracentrifugation; Dihydrodipicolinate synthase; Molecular dynamics simulations; Oligomer; Quaternary structure; Sedimentation equilibrium; Sedimentation velocity; Self-association; Small angle X-ray scattering; X-ray crystallography.