Seminar Series

Insights into Enzyme Allosteric Inhibition Mechanisms using Computational Studies

Speaker

Eric Lang Final Ph.D. Seminar

Institute

Time & Place

Fri, 01 Jul 2016 11:00:00 NZST in Rutherford Room 531

All are welcome

Abstract

Allostery, the process by which action of an effector at one site of the protein provokes a functional response at a distant site, is critical in the regulation of metabolic pathways. Yet, despite its importance, allostery remains enigmatic and little detailed information is known about how the function of the protein is affected, how the allosteric signal is communicated or how allosteric regulation evolves in a protein.

In this presentation, new insights into the understanding of allostery will be provided by studying different allosteric regulation mechanisms using a variety of computational methods, including molecular dynamics simulations. The metabolic enzyme 3-deoxy-D-arabino-heptulosonate 7- phosphate synthase (DAH7PS), which catalyses the first step of the shikimate pathway, is used as a model enzyme for allostery due to the unprecedented variety of allosteric regulation mechanisms this protein can deploy, from large domain movements to dynamic allostery, representing an ideal playground to study allostery.

The implications of this work will be discussed in the general context of allosteric regulation mechanisms and evolution.