6GQV

Cryo-EM recosntruction of yeast 80S ribosome in complex with mRNA, tRNA and eEF2 (GMPPCP)

これはPDB形式変換不可エントリーです。

6GQV の概要

• エントリーDOI: 10.2210/pdb6gqv/pdb
• 関連するPDBエントリー: 6GQ1 6GQB
• EMDBエントリー: 0047 0048 0049
• 分子名称: 25S ribosomal RNA, 60S ribosomal protein L6-A, 60S ribosomal protein L7-A, ... (86 entities in total)
• 機能のキーワード: eukaryotic 80s ribosome, diphthamide, eef2, translation fidelity, mrna-trna translocation, ribosome
• 由来する生物種: Saccharomyces cerevisiae; 詳細
• タンパク質・核酸の鎖数: 84
• 化学式量合計: 3191429.53

構造登録者

Pellegrino, S.,Yusupov, M.,Yusupova, G.,Hashem, Y. (登録日: 2018-06-08, 公開日: 2018-07-11, 最終更新日: 2018-08-08)

主引用文献

Pellegrino, S.,Demeshkina, N.,Mancera-Martinez, E.,Melnikov, S.,Simonetti, A.,Myasnikov, A.,Yusupov, M.,Yusupova, G.,Hashem, Y.
Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance.
J. Mol. Biol., 430:2677-2687, 2018

PubMed Abstract: One of the most critical steps of protein biosynthesis is the coupled movement of mRNA, which encodes genetic information, with tRNAs on the ribosome. In eukaryotes, this process is catalyzed by a conserved G-protein, the elongation factor 2 (eEF2), which carries a unique post-translational modification, called diphthamide, found in all eukaryotic species. Here we present near-atomic resolution cryo-electron microscopy structures of yeast 80S ribosome complexes containing mRNA, tRNA and eEF2 trapped in different GTP-hydrolysis states which provide further structural insights into the role of diphthamide in the mechanism of translation fidelity in eukaryotes.

PubMed: 29886014
DOI: 10.1016/j.jmb.2018.06.006

実験手法

ELECTRON MICROSCOPY (4 Å)