3J0E

Models for the T. thermophilus ribosome recycling factor and the E. coli elongation factor G bound to the E. coli post-termination complex

3J0E の概要

• エントリーDOI: 10.2210/pdb3j0e/pdb
• EMDBエントリー: 1917 1918
• 分子名称: ribosomal 23S RNA, ribosomal 16S RNA, 30S ribosomal protein S12, ... (9 entities in total)
• 機能のキーワード: ribosome, ribosome recycling factor, elongation factor g, translation
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 146842.86

構造登録者

Yokoyama, T.,Shaikh, T.R.,Iwakura, N.,Kaji, H.,Kaji, A.,Agrawal, R.K. (登録日: 2011-06-29, 公開日: 2012-04-25, 最終更新日: 2024-02-21)

主引用文献

Yokoyama, T.,Shaikh, T.R.,Iwakura, N.,Kaji, H.,Kaji, A.,Agrawal, R.K.
Structural insights into initial and intermediate steps of the ribosome-recycling process.
Embo J., 31:1836-1846, 2012

PubMed Abstract: The ribosome-recycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-termination complex (PoTC) into mRNA, tRNA, and two ribosomal subunits. We have determined cryo-electron microscopic structures of the PoTC·RRF complex, with and without EF-G. We find that domain II of RRF initially interacts with universally conserved residues of the 23S rRNA helices 43 and 95, and protein L11 within the 50S ribosomal subunit. Upon EF-G binding, both RRF and tRNA are driven towards the tRNA-exit (E) site, with a large rotational movement of domain II of RRF towards the 30S ribosomal subunit. During this intermediate step of the recycling process, domain II of RRF and domain IV of EF-G adopt hitherto unknown conformations. Furthermore, binding of EF-G to the PoTC·RRF complex reverts the ribosome from ratcheted to unratcheted state. These results suggest that (i) the ribosomal intersubunit reorganizations upon RRF binding and subsequent EF-G binding could be instrumental in destabilizing the PoTC and (ii) the modes of action of EF-G during tRNA translocation and ribosome-recycling steps are markedly different.

PubMed: 22388519
DOI: 10.1038/emboj.2012.22

実験手法

ELECTRON MICROSCOPY (9.9 Å)