5NWY

2.9 A cryo-EM structure of VemP-stalled ribosome-nascent chain complex

これはPDB形式変換不可エントリーです。

5NWY の概要

• エントリーDOI: 10.2210/pdb5nwy/pdb
• EMDBエントリー: 3713
• 分子名称: VemP nascent chain, 50S ribosomal protein L11, 50S ribosomal protein L13, ... (56 entities in total)
• 機能のキーワード: vemp-src, peptidyltransferase center, ribosomal exit tunnel, helix-loop-helix. ribosome, 70s, ribosome stalling, arrest peptide, ribosome
• 由来する生物種: Vibrio alginolyticus; 詳細
• タンパク質・核酸の鎖数: 56
• 化学式量合計: 2195557.10

構造登録者

Su, T.,Cheng, J.,Sohmen, D.,Hedman, R.,Berninghausen, O.,von Heijne, G.,Wilson, D.N.,Beckmann, R. (登録日: 2017-05-08, 公開日: 2017-07-19, 最終更新日: 2024-10-16)

主引用文献

Su, T.,Cheng, J.,Sohmen, D.,Hedman, R.,Berninghausen, O.,von Heijne, G.,Wilson, D.N.,Beckmann, R.
The force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling.
Elife, 6:-, 2017

PubMed Abstract: Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modulate the rate of translation and induce translational arrest to regulate expression of downstream genes. The ribosomal tunnel also provides a protected environment for initial protein folding events. Here, we present a 2.9 Å cryo-electron microscopy structure of a ribosome stalled during translation of the extremely compacted VemP nascent chain. The nascent chain forms two α-helices connected by an α-turn and a loop, enabling a total of 37 amino acids to be observed within the first 50-55 Å of the exit tunnel. The structure reveals how α-helix formation directly within the peptidyltransferase center of the ribosome interferes with aminoacyl-tRNA accommodation, suggesting that during canonical translation, a major role of the exit tunnel is to prevent excessive secondary structure formation that can interfere with the peptidyltransferase activity of the ribosome.

PubMed: 28556777
DOI: 10.7554/eLife.25642

実験手法

ELECTRON MICROSCOPY (2.9 Å)