5J3Q

Crystal structure of S. pombe Dcp1:Edc1 mRNA decapping complex

5J3Q の概要

• エントリーDOI: 10.2210/pdb5j3q/pdb
• 関連するPDBエントリー: 5J3T 5J3Y
• 分子名称: mRNA-decapping enzyme subunit 1, Edc1 (3 entities in total)
• 機能のキーワード: hydrolase, decapping, mrna decay, evh1
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast); 詳細
• 細胞内の位置: Cytoplasm : Q9P805
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 36073.08

構造登録者

Valkov, E.,Muthukumar, S.,Chang, C.T.,Jonas, S.,Weichenrieder, O.,Izaurralde, E. (登録日: 2016-03-31, 公開日: 2016-05-18, 最終更新日: 2024-01-10)

主引用文献

Valkov, E.,Muthukumar, S.,Chang, C.T.,Jonas, S.,Weichenrieder, O.,Izaurralde, E.
Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation.
Nat.Struct.Mol.Biol., 23:574-579, 2016

PubMed Abstract: The removal of the mRNA 5' cap (decapping) by Dcp2 shuts down translation and commits mRNA to full degradation. Dcp2 activity is enhanced by activator proteins such as Dcp1 and Edc1. However, owing to conformational flexibility, the active conformation of Dcp2 and the mechanism of decapping activation have remained unknown. Here, we report a 1.6-Å-resolution crystal structure of the Schizosaccharomyces pombe Dcp2-Dcp1 heterodimer in an unprecedented conformation that is tied together by an intrinsically disordered peptide from Edc1. In this ternary complex, an unforeseen rotation of the Dcp2 catalytic domain allows residues from both Dcp2 and Dcp1 to cooperate in RNA binding, thus explaining decapping activation by increased substrate affinity. The architecture of the Dcp2-Dcp1-Edc1 complex provides a rationale for the conservation of a sequence motif in Edc1 that is also present in unrelated decapping activators, thus indicating that the presently described mechanism of decapping activation is evolutionarily conserved.

PubMed: 27183195
DOI: 10.1038/nsmb.3232

実験手法

X-RAY DIFFRACTION (1.87 Å)