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

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Otherpeer-review

14 Citations (Scopus)

Abstract

Here, we review recent studies aimed at defining the importance of quaternary structureto a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate thecomplementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugationwith enzyme kinetics, in vitro mutagenesis, macromolecular crystallography,small angle X-ray scattering, and molecular dynamics simulations, to demonstratethe role of subunit self-association in facilitating protein dynamics and enzyme function.This multitechnique approach has yielded new insights into the molecular evolution ofprotein quaternary structure.
Original languageEnglish
Title of host publicationMethods in enzymology
Subtitle of host publicationAnalytical ultracentrifugation
EditorsJohn N. Abelson, Melvin I. Simon, Anna Marie Pyle, David W. Christianson
Place of PublicationNew York
PublisherAcademic Press
Pages205-223
Number of pages19
Volume562
ISBN (Print)9780128029084
DOIs
Publication statusPublished - 2015

Keywords

  • analytical ultracentrifugation
  • dihydrodipicolinate synthase
  • molecular dynamics simulations
  • oligomer
  • quaternary structure
  • self-association
  • sedimentation equilibrium
  • sedimentation velocity
  • small angle x-ray scattering
  • x-ray crystallography

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