6OGG

70S termination complex with RF2 bound to the UGA codon. Rotated ribosome with RF2 bound (Structure IV).

これはPDB形式変換不可エントリーです。

6OGG の概要

• エントリーDOI: 10.2210/pdb6ogg/pdb
• EMDBエントリー: 20057
• 分子名称: 50S ribosomal protein L2, 50S ribosomal protein L16, 50S ribosomal protein L17, ... (55 entities in total)
• 機能のキーワード: ribosome recycling, translation termination, rf2, intersubunit rotation, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 55
• 化学式量合計: 2228594.25

構造登録者

Svidritskiy, E.,Demo, G.,Loveland, A.B.,Xu, C.,Korostelev, A.A. (登録日: 2019-04-02, 公開日: 2019-09-25, 最終更新日: 2024-03-20)

主引用文献

Svidritskiy, E.,Demo, G.,Loveland, A.B.,Xu, C.,Korostelev, A.A.
Extensive ribosome and RF2 rearrangements during translation termination.
Elife, 8:-, 2019

PubMed Abstract: Protein synthesis ends when a ribosome reaches an mRNA stop codon. Release factors (RFs) decode the stop codon, hydrolyze peptidyl-tRNA to release the nascent protein, and then dissociate to allow ribosome recycling. To visualize termination by RF2, we resolved a cryo-EM ensemble of 70S•RF2 structures at up to 3.3 Å in a single sample. Five structures suggest a highly dynamic termination pathway. Upon peptidyl-tRNA hydrolysis, the CCA end of deacyl-tRNA departs from the peptidyl transferase center. The catalytic GGQ loop of RF2 is rearranged into a long β-hairpin that plugs the peptide tunnel, biasing a nascent protein toward the ribosome exit. Ribosomal intersubunit rotation destabilizes the catalytic RF2 domain on the 50S subunit and disassembles the central intersubunit bridge B2a, resulting in RF2 departure. Our structures visualize how local rearrangements and spontaneous inter-subunit rotation poise the newly-made protein and RF2 to dissociate in preparation for ribosome recycling.

PubMed: 31513010
DOI: 10.7554/eLife.46850

実験手法

ELECTRON MICROSCOPY (4.2 Å)