8J7R

Cryo-EM structure of the J-K-St region of EMCV IRES in complex with eIF4G-HEAT1 and eIF4A (J-K-St/eIF4G focused)

8J7R の概要

• エントリーDOI: 10.2210/pdb8j7r/pdb
• 関連するPDBエントリー: 8HUJ
• EMDBエントリー: 35041 36046
• 分子名称: Eukaryotic translation initiation factor 4 gamma 1, IRES RNA (J-K-St), MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: translation initiation factors, translation, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66698.33

構造登録者

Suzuki, H.,Fujiyoshi, Y.,Imai, S.,Shimada, I. (登録日: 2023-04-28, 公開日: 2023-08-02, 最終更新日: 2023-09-13)

主引用文献

Imai, S.,Suzuki, H.,Fujiyoshi, Y.,Shimada, I.
Dynamically regulated two-site interaction of viral RNA to capture host translation initiation factor.
Nat Commun, 14:4977-4977, 2023

PubMed Abstract: Many RNA viruses employ internal ribosome entry sites (IRESs) in their genomic RNA to commandeer the host's translational machinery for replication. The IRES from encephalomyocarditis virus (EMCV) interacts with eukaryotic translation initiation factor 4 G (eIF4G), recruiting the ribosomal subunit for translation. Here, we analyze the three-dimensional structure of the complex composed of EMCV IRES, the HEAT1 domain fragment of eIF4G, and eIF4A, by cryo-electron microscopy. Two distinct eIF4G-interacting domains on the IRES are identified, and complex formation changes the angle therebetween. Further, we explore the dynamics of these domains by using solution NMR spectroscopy, revealing conformational equilibria in the microsecond to millisecond timescale. In the lowly-populated conformations, the base-pairing register of one domain is shifted with the structural transition of the three-way junction, as in the complex structure. Our study provides insights into the viral RNA's sophisticated strategy for optimal docking to hijack the host protein.

PubMed: 37640715
DOI: 10.1038/s41467-023-40582-6

実験手法

ELECTRON MICROSCOPY (3.7 Å)