1ST4

Structure of DcpS bound to m7GpppA

1ST4 の概要

• エントリーDOI: 10.2210/pdb1st4/pdb
• 関連するPDBエントリー: 1ST0
• 分子名称: mRNA decapping enzyme, P1-7-METHYLGUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE, YTTRIUM (III) ION, ... (4 entities in total)
• 機能のキーワード: rna decay, exosome, decapping, hit protein, messenger rna, mrna, cap, rna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q96C86
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79119.00

構造登録者

Gu, M.,Fabrega, C.,Liu, S.W.,Liu, H.,Kiledjian, M.,Lima, C.D. (登録日: 2004-03-24, 公開日: 2004-04-13, 最終更新日: 2023-08-23)

主引用文献

Gu, M.,Fabrega, C.,Liu, S.W.,Liu, H.,Kiledjian, M.,Lima, C.D.
Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity
Mol.Cell, 14:67-80, 2004

PubMed Abstract: Complete removal of residual N-7 guanine cap from degraded messenger RNA is necessary to prevent accumulation of intermediates that might interfere with RNA processing, export, and translation. The human scavenger decapping enzyme, DcpS, catalyzes residual cap hydrolysis following mRNA degradation, releasing N-7 methyl guanosine monophosphate and 5'-diphosphate terminated cap or mRNA products. DcpS structures bound to m(7)GpppG or m(7)GpppA reveal an asymmetric DcpS dimer that simultaneously creates an open nonproductive DcpS-cap complex and a closed productive DcpS-cap complex that alternate via 30 A domain movements. Structural and biochemical analysis suggests an autoregulatory mechanism whereby premature decapping mRNA is prevented by blocking the conformational changes that are required to form a closed productive active site capable of cap hydrolysis.

PubMed: 15068804
DOI: 10.1016/S1097-2765(04)00180-7

実験手法

X-RAY DIFFRACTION (2.02 Å)