Quaternary Structure Analyses of an Essential Oligomeric Enzyme
Tatiana P Soares da Costa, Janni B Christensen, Sebastien Desbois, Shane E Gordon, Ruchi Gupta, Campbell J Hogan, Tao G Nelson, Matthew T Downton, Chamodi K Gardhi, Belinda M Abbott, John Wagner, Santosh Panjikar, Matthew A Perugini, JL Cole (ed.)
Methods in Enzymology | ELSEVIER ACADEMIC PRESS INC | Published : 2015
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.