Soares da Costa Tatiana P, Christensen Janni B, Desbois Sebastien, Gordon Shane E, Gupta Ruchi, Hogan Campbell J, Nelson Tao G, Downton Matthew T, Gardhi Chamodi K, Abbott Belinda M, Wagner John, Panjikar Santosh, Perugini Matthew A
Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia.
IBM Research Collaboratory for Life Sciences-Melbourne, Victorian Life Sciences Computation Initiative, Carlton, Victoria, Australia.
Methods Enzymol. 2015;562:205-23. doi: 10.1016/bs.mie.2015.06.020. Epub 2015 Aug 13.
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.
在此,我们回顾了近期旨在确定四级结构对模型寡聚酶二氢二吡啶甲酸合酶重要性的研究。这将说明将分析超速离心技术与酶动力学、体外诱变、大分子晶体学、小角X射线散射和分子动力学模拟相结合所产生的互补和协同结果,以证明亚基自缔合在促进蛋白质动力学和酶功能方面的作用。这种多技术方法为蛋白质四级结构的分子进化带来了新的见解。