3J6Q

Identification of the active sites in the methyltransferases of a transcribing dsRNA virus

3J6Q の概要

• エントリーDOI: 10.2210/pdb3j6q/pdb
• EMDBエントリー: 5926
• 分子名称: Structural protein VP3, S-ADENOSYL-L-HOMOCYSTEINE (2 entities in total)
• 機能のキーワード: dsrna virus, reoviridae, rna capping, rna methyltransferase, virus
• 由来する生物種: Bombyx mori cypovirus 1 (BmCPV)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 606294.03

構造登録者

Zhu, B.,Yang, C.,Liu, H.,Cheng, L.,Song, F.,Zeng, S.,Huang, X.,Ji, G.,Zhu, P. (登録日: 2014-03-20, 公開日: 2014-10-08, 最終更新日: 2025-04-09)

主引用文献

Zhu, B.,Yang, C.,Liu, H.,Cheng, L.,Song, F.,Zeng, S.,Huang, X.,Ji, G.,Zhu, P.
Identification of the active sites in the methyltransferases of a transcribing dsRNA virus.
J.Mol.Biol., 426:2167-2174, 2014

PubMed Abstract: Many double-stranded RNA (dsRNA) viruses are capable of transcribing and capping RNA within a stable icosahedral viral capsid. The turret of turreted dsRNA viruses belonging to the family Reoviridae is formed by five copies of the turret protein, which contains domains with both 7-N-methyltransferase and 2'-O-methyltransferase activities, and serves to catalyze the methylation reactions during RNA capping. Cypovirus of the family Reoviridae provides a good model system for studying the methylation reactions in dsRNA viruses. Here, we present the structure of a transcribing cypovirus to a resolution of ~3.8Å by cryo-electron microscopy. The binding sites for both S-adenosyl-L-methionine and RNA in the two methyltransferases of the turret were identified. Structural analysis of the turret in complex with RNA revealed a pathway through which the RNA molecule reaches the active sites of the two methyltransferases before it is released into the cytoplasm. The pathway shows that RNA capping reactions occur in the active sites of different turret protein monomers, suggesting that RNA capping requires concerted efforts by at least three turret protein monomers. Thus, the turret structure provides novel insights into the precise mechanisms of RNA methylation.

PubMed: 24690366
DOI: 10.1016/j.jmb.2014.03.013

実験手法

ELECTRON MICROSCOPY (3.8 Å)