Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis

Jeffrey S. Mugridge; Ryan W. Tibble; Marcin Ziemniak; Jacek Jemielity; John D. Gross

doi:10.1038/s41467-018-03536-x

Nature Communications (Mar 2018)

Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis

Jeffrey S. Mugridge,
Ryan W. Tibble,
Marcin Ziemniak,
Jacek Jemielity,
John D. Gross

Affiliations

Jeffrey S. Mugridge: Department of Pharmaceutical Chemistry, University of California, San Francisco
Ryan W. Tibble: Department of Pharmaceutical Chemistry, University of California, San Francisco
Marcin Ziemniak: Division of Biophysics, Institute of Experimental Physics, Faculty of Physics, University of Warsaw
Jacek Jemielity: Centre of New Technologies, University of Warsaw
John D. Gross: Department of Pharmaceutical Chemistry, University of California, San Francisco

DOI: https://doi.org/10.1038/s41467-018-03536-x
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 10

Abstract

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The decapping enzyme Dcp2 removes the 5′ eukaryotic cap from mRNA transcripts and acts in concert with its essential activator Dcp1 and various coactivators. Here the authors present the structure of the fully-activated mRNA decapping complex, which reveals how Dcp2 recognizes the cap substrate and coactivators Edc1 and Edc3 activate catalysis.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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