8PEG

Escherichia coli paused disome complex (queueing 70S non-rotated closed PRE state)

これはPDB形式変換不可エントリーです。

8PEG の概要

• エントリーDOI: 10.2210/pdb8peg/pdb
• EMDBエントリー: 17631
• 分子名称: 50S ribosomal protein L36, 16S ribosomal RNA, Small ribosomal subunit protein uS2, ... (64 entities in total)
• 機能のキーワード: translation, disome, collision, pure system, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 61
• 化学式量合計: 2352287.01

構造登録者

Fluegel, T.,Schacherl, M. (登録日: 2023-06-13, 公開日: 2024-03-06, 最終更新日: 2025-03-12)

主引用文献

Flugel, T.,Schacherl, M.,Unbehaun, A.,Schroeer, B.,Dabrowski, M.,Burger, J.,Mielke, T.,Sprink, T.,Diebolder, C.A.,Guillen Schlippe, Y.V.,Spahn, C.M.T.
Transient disome complex formation in native polysomes during ongoing protein synthesis captured by cryo-EM.
Nat Commun, 15:1756-1756, 2024

PubMed Abstract: Structural studies of translating ribosomes traditionally rely on in vitro assembly and stalling of ribosomes in defined states. To comprehensively visualize bacterial translation, we reactivated ex vivo-derived E. coli polysomes in the PURE in vitro translation system and analyzed the actively elongating polysomes by cryo-EM. We find that 31% of 70S ribosomes assemble into disome complexes that represent eight distinct functional states including decoding and termination intermediates, and a pre-nucleophilic attack state. The functional diversity of disome complexes together with RNase digest experiments suggests that paused disome complexes transiently form during ongoing elongation. Structural analysis revealed five disome interfaces between leading and queueing ribosomes that undergo rearrangements as the leading ribosome traverses through the elongation cycle. Our findings reveal at the molecular level how bL9's CTD obstructs the factor binding site of queueing ribosomes to thwart harmful collisions and illustrate how translation dynamics reshape inter-ribosomal contacts.

PubMed: 38409277
DOI: 10.1038/s41467-024-46092-3

実験手法

ELECTRON MICROSCOPY (3.3 Å)