Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.

ABSTRACT: Crystal structures of enzymes are indispensable to understanding their mechanisms on a molecular level. It, however, remains challenging to determine which structures are adopted in solution, especially for dynamic complexes. Here, we study the bilobed decapping enzyme Dcp2 that removes the 5' cap structure from eukaryotic mRNA and thereby efficiently terminates gene expression. The numerous Dcp2 structures can be grouped into six states where the domain orientation between the catalytic and regulatory domains significantly differs. Despite this wealth of structural information it is not possible to correlate these states with the catalytic cycle or the activity of the enzyme. Using methyl transverse relaxation-optimized NMR spectroscopy, we demonstrate that only three of the six domain or

SUBMITTER: Wurm JP 

PROVIDER: S-EPMC5468633 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature