Allosteric Impact of the Variable Insert Loop in Vaccinia H1-Related (VHR) Phosphatase.

ABSTRACT: Dynamics and conformational motions are important to the activity of enzymes, including protein tyrosine phosphatases. These motions often extend to regions outside the active site, called allosteric regions. In the tyrosine phosphatase Vaccinia H1-related (VHR) enzyme, we demonstrate the importance of the allosteric interaction between the variable insert region and the active-site loops in VHR. These studies include solution nuclear magnetic resonance, computation, steady-state, and rapid kinetic measurements. Overall, the data indicate concerted millisecond motions exist between the variable insert and the catalytic acid loop in wild-type (WT) VHR. The 150 ns computation studies show a flexible acid loop in WT VHR that opens during the simulation from its initial closed structure

SUBMITTER: Beaumont VA 

PROVIDER: S-EPMC7364816 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature