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5LW7

S. solfataricus ABCE1 post-splitting state

5LW7 の概要
エントリーDOI10.2210/pdb5lw7/pdb
関連するPDBエントリー4V6U
EMDBエントリー4113
分子名称ABC transporter ATP-binding protein, IRON/SULFUR CLUSTER (2 entities in total)
機能のキーワードabce1, recycling, 30s, ribosome
由来する生物種Pyrococcus abyssi (strain GE5 / Orsay)
タンパク質・核酸の鎖数1
化学式量合計67989.55
構造登録者
Heuer, A.,Gerovac, M.,Beckmann, R.,Tampe, R. (登録日: 2016-09-15, 公開日: 2016-11-16, 最終更新日: 2024-11-13)
主引用文献Kiosze-Becker, K.,Ori, A.,Gerovac, M.,Heuer, A.,Nurenberg-Goloub, E.,Rashid, U.J.,Becker, T.,Beckmann, R.,Beck, M.,Tampe, R.
Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry.
Nat Commun, 7:13248-13248, 2016
Cited by
PubMed Abstract: Ribosome recycling orchestrated by the ATP binding cassette (ABC) protein ABCE1 can be considered as the final-or the first-step within the cyclic process of protein synthesis, connecting translation termination and mRNA surveillance with re-initiation. An ATP-dependent tweezer-like motion of the nucleotide-binding domains in ABCE1 transfers mechanical energy to the ribosome and tears the ribosome subunits apart. The post-recycling complex (PRC) then re-initiates mRNA translation. Here, we probed the so far unknown architecture of the 1-MDa PRC (40S/30S·ABCE1) by chemical cross-linking and mass spectrometry (XL-MS). Our study reveals ABCE1 bound to the translational factor-binding (GTPase) site with multiple cross-link contacts of the helix-loop-helix motif to the S24e ribosomal protein. Cross-linking of the FeS cluster domain to the ribosomal protein S12 substantiates an extreme lever-arm movement of the FeS cluster domain during ribosome recycling. We were thus able to reconstitute and structurally analyse a key complex in the translational cycle, resembling the link between translation initiation and ribosome recycling.
PubMed: 27824037
DOI: 10.1038/ncomms13248
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (17 Å)
構造検証レポート
Validation report summary of 5lw7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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