The role of oligomerization and cooperative regulation in protein function: the case of tryptophan synthase.

ABSTRACT: The oligomerization/co-localization of protein complexes and their cooperative regulation in protein function is a key feature in many biological systems. The synergistic regulation in different subunits often enhances the functional properties of the multi-enzyme complex. The present study used molecular dynamics and Brownian dynamics simulations to study the effects of allostery, oligomerization and intermediate channeling on enhancing the protein function of tryptophan synthase (TRPS). TRPS uses a set of α/β-dimeric units to catalyze the last two steps of L-tryptophan biosynthesis, and the rate is remarkably slower in the isolated monomers. Our work shows that without their binding partner, the isolated monomers are stable and more rigid. The substrates can form fairly stable interactio

SUBMITTER: Fatmi MQ 

PROVIDER: S-EPMC2978696 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature