6IP5

Cryo-EM structure of the CMV-stalled human 80S ribosome (Structure ii)

これはPDB形式変換不可エントリーです。

6IP5 の概要

• エントリーDOI: 10.2210/pdb6ip5/pdb
• EMDBエントリー: 9699 9701 9702 9703 9704
• 分子名称: 28S ribosomal RNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (83 entities in total)
• 機能のキーワード: ribosome, translation
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 84
• 化学式量合計: 3857099.05

構造登録者

Yokoyama, T.,Shigematsu, H.,Shirouzu, M.,Imataka, H.,Ito, T. (登録日: 2018-11-02, 公開日: 2019-05-29, 最終更新日: 2024-11-13)

主引用文献

Yokoyama, T.,Machida, K.,Iwasaki, W.,Shigeta, T.,Nishimoto, M.,Takahashi, M.,Sakamoto, A.,Yonemochi, M.,Harada, Y.,Shigematsu, H.,Shirouzu, M.,Tadakuma, H.,Imataka, H.,Ito, T.
HCV IRES Captures an Actively Translating 80S Ribosome.
Mol.Cell, 74:1205-1214.e8, 2019

PubMed Abstract: Translation initiation of hepatitis C virus (HCV) genomic RNA is induced by an internal ribosome entry site (IRES). Our cryoelectron microscopy (cryo-EM) analysis revealed that the HCV IRES binds to the solvent side of the 40S platform of the cap-dependently translating 80S ribosome. Furthermore, we obtained the cryo-EM structures of the HCV IRES capturing the 40S subunit of the IRES-dependently translating 80S ribosome. In the elucidated structures, the HCV IRES "body," consisting of domain III except for subdomain IIIb, binds to the 40S subunit, while the "long arm," consisting of domain II, remains flexible and does not impede the ongoing translation. Biochemical experiments revealed that the cap-dependently translating ribosome becomes a better substrate for the HCV IRES than the free ribosome. Therefore, the HCV IRES is likely to efficiently induce the translation initiation of its downstream mRNA with the captured translating ribosome as soon as the ongoing translation terminates.

PubMed: 31080011
DOI: 10.1016/j.molcel.2019.04.022

実験手法

ELECTRON MICROSCOPY (3.9 Å)