| Literature DB >> 26412653 |
Tatiana P Soares da Costa1, Janni B Christensen1, Sebastien Desbois1, Shane E Gordon1, Ruchi Gupta1, Campbell J Hogan1, Tao G Nelson1, Matthew T Downton2, Chamodi K Gardhi3, Belinda M Abbott3, John Wagner2, Santosh Panjikar4, Matthew A Perugini5.
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
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Year: 2015 PMID: 26412653 DOI: 10.1016/bs.mie.2015.06.020
Source DB: PubMed Journal: Methods Enzymol ISSN: 0076-6879 Impact factor: 1.600