4J7M

Crystal structure of mouse DXO in complex with substrate mimic RNA and calcium ion

4J7M の概要

• エントリーDOI: 10.2210/pdb4j7m/pdb
• 関連するPDBエントリー: 3FQI 3FQJ 4J7L 4J7N
• 分子名称: Protein Dom3Z, RNA (5'-R(P*UP*(U37)P*(U37)P*UP*U)-3'), URIDINE 3',5'-BIS(DIHYDROGEN PHOSPHATE), ... (5 entities in total)
• 機能のキーワード: decapping, 5'-3' exoribonuclease, hydrolase, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Nucleus (By similarity): O70348
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45498.94

構造登録者

Chang, J.H.,Tong, L. (登録日: 2013-02-13, 公開日: 2013-03-27, 最終更新日: 2024-02-28)

主引用文献

Jiao, X.,Chang, J.H.,Kilic, T.,Tong, L.,Kiledjian, M.
A mammalian pre-mRNA 5' end capping quality control mechanism and an unexpected link of capping to pre-mRNA processing.
Mol.Cell, 50:104-115, 2013

PubMed Abstract: Recently, we reported that two homologous yeast proteins, Rai1 and Dxo1, function in a quality control mechanism to clear cells of incompletely 5' end-capped messenger RNAs (mRNAs). Here, we report that their mammalian homolog, Dom3Z (referred to as DXO), possesses pyrophosphohydrolase, decapping, and 5'-to-3' exoribonuclease activities. Surprisingly, we found that DXO preferentially degrades defectively capped pre-mRNAs in cells. Additional studies show that incompletely capped pre-mRNAs are inefficiently spliced at all introns, a fact that contrasts with current understanding, and are also poorly cleaved for polyadenylation. Crystal structures of DXO in complex with substrate mimic and products at a resolution of up to 1.5Å provide elegant insights into the catalytic mechanism and molecular basis for their three apparently distinct activities. Our data reveal a pre-mRNA 5' end capping quality control mechanism in mammalian cells, indicating DXO as the central player for this mechanism, and demonstrate an unexpected intimate link between proper 5' end capping and subsequent pre-mRNA processing.

PubMed: 23523372
DOI: 10.1016/j.molcel.2013.02.017

実験手法

X-RAY DIFFRACTION (1.7 Å)