Ontology highlight
ABSTRACT:
SUBMITTER: Mugridge JS
PROVIDER: S-EPMC5113729 | biostudies-literature | 2016 Nov
REPOSITORIES: biostudies-literature
Mugridge Jeffrey S JS Ziemniak Marcin M Jemielity Jacek J Gross John D JD
Nature structural & molecular biology 20161003 11
Removal of the 5' cap on mRNA by the decapping enzyme Dcp2 is a critical step in 5'-to-3' mRNA decay. Understanding the structural basis of Dcp2 activity has been a challenge because Dcp2 is dynamic and has weak affinity for the cap substrate. Here we present a 2.6-Å-resolution crystal structure of a heterotrimer of fission yeast Dcp2, its essential activator Dcp1, and the human NMD cofactor PNRC2, in complex with a tight-binding cap analog. Cap binding is accompanied by a conformational change ...[more]