6AWD

Structure of 30S (S1 depleted) ribosomal subunit and RNA polymerase complex

これはPDB形式変換不可エントリーです。

6AWD の概要

• エントリーDOI: 10.2210/pdb6awd/pdb
• EMDBエントリー: 7014 7015 7016
• 分子名称: 16S rRNA, 30S ribosomal protein S6, 30S ribosomal protein S7, ... (25 entities in total)
• 機能のキーワード: 30s subunit, rna polymerase, complex, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 1126292.60

構造登録者

Demo, G.,Rasouly, A.,Vasilyev, N.,Loveland, A.B.,Diaz-Avalos, R.,Grigorieff, N.,Nudler, E.,Korostelev, A.A. (登録日: 2017-09-05, 公開日: 2017-10-18, 最終更新日: 2024-03-13)

主引用文献

Demo, G.,Rasouly, A.,Vasilyev, N.,Svetlov, V.,Loveland, A.B.,Diaz-Avalos, R.,Grigorieff, N.,Nudler, E.,Korostelev, A.A.
Structure of RNA polymerase bound to ribosomal 30S subunit.
Elife, 6:-, 2017

PubMed Abstract: In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of RNAP core bound to the small ribosomal 30S subunit. The complex is stable under cell-like ionic conditions, consistent with functional interaction between RNAP and the 30S subunit. The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the 30S subunit. Ribosomal protein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in directing mRNAs onto the ribosome. The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting different functional states during transcription-translation coupling. The architecture of the 30S•RNAP complex provides a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation.

PubMed: 29027901
DOI: 10.7554/eLife.28560

実験手法

ELECTRON MICROSCOPY (8.1 Å)