6TMF

Structure of an archaeal ABCE1-bound ribosomal post-splitting complex

6TMF の概要

• エントリーDOI: 10.2210/pdb6tmf/pdb
• EMDBエントリー: 10519
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S8, 30S ribosomal protein S8e, ... (34 entities in total)
• 機能のキーワード: abc proteins, ribosome recycling, translation, ribosome
• 由来する生物種: Saccharolobus solfataricus; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 962388.30

構造登録者

Kratzat, H.,Becker, T.,Tampe, R.,Beckmann, R. (登録日: 2019-12-04, 公開日: 2020-02-12, 最終更新日: 2024-05-22)

主引用文献

Nurenberg-Goloub, E.,Kratzat, H.,Heinemann, H.,Heuer, A.,Kotter, P.,Berninghausen, O.,Becker, T.,Tampe, R.,Beckmann, R.
Molecular analysis of the ribosome recycling factor ABCE1 bound to the 30S post-splitting complex.
Embo J., 39:e103788-e103788, 2020

PubMed Abstract: Ribosome recycling by the twin-ATPase ABCE1 is a key regulatory process in mRNA translation and surveillance and in ribosome-associated protein quality control in Eukarya and Archaea. Here, we captured the archaeal 30S ribosome post-splitting complex at 2.8 Å resolution by cryo-electron microscopy. The structure reveals the dynamic behavior of structural motifs unique to ABCE1, which ultimately leads to ribosome splitting. More specifically, we provide molecular details on how conformational rearrangements of the iron-sulfur cluster domain and hinge regions of ABCE1 are linked to closure of its nucleotide-binding sites. The combination of mutational and functional analyses uncovers an intricate allosteric network between the ribosome, regulatory domains of ABCE1, and its two structurally and functionally asymmetric ATP-binding sites. Based on these data, we propose a refined model of how signals from the ribosome are integrated into the ATPase cycle of ABCE1 to orchestrate ribosome recycling.

PubMed: 32064661
DOI: 10.15252/embj.2019103788

実験手法

ELECTRON MICROSCOPY (2.8 Å)