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Methods Enzymol. 2015;562:205-23. doi: 10.1016/bs.mie.2015.06.020. Epub 2015 Aug 13.

Quaternary Structure Analyses of an Essential Oligomeric Enzyme.

Author information

1
Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia.
2
IBM Research Collaboratory for Life Sciences-Melbourne, Victorian Life Sciences Computation Initiative, Carlton, Victoria, Australia.
3
Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne Victoria, Australia.
4
Australian Synchrotron, Clayton, Victoria, Australia; Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.
5
Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia. Electronic address: m.perugini@latrobe.edu.au.

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

PMID:
26412653
DOI:
10.1016/bs.mie.2015.06.020
[Indexed for MEDLINE]

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