4CRN

Cryo-EM of a pretermination complex with eRF1 and eRF3

4CRN の概要

• エントリーDOI: 10.2210/pdb4crn/pdb
• 関連するPDBエントリー: 4CRM
• EMDBエントリー: 2597
• 分子名称: ERF3 IN RIBOSOME BOUND ERF1-ERF3-GDPNP COMPLEX, ERF1 IN RIBOSOME-BOUND ERF1-ERF3-GDPNP COMPLEX, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER (3 entities in total)
• 機能のキーワード: translation, termination, cryo-em
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Cytoplasm : P05453 P12385
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97395.54

構造登録者

Preis, A.,Heuer, A.,Barrio-Garcia, C.,Hauser, A.,Eyler, D.,Berninghausen, O.,Green, R.,Becker, T.,Beckmann, R. (登録日: 2014-02-28, 公開日: 2014-07-23, 最終更新日: 2024-05-08)

主引用文献

Preis, A.,Heuer, A.,Barrio-Garcia, C.,Hauser, A.,Eyler, D.E.,Berninghausen, O.,Green, R.,Becker, T.,Beckmann, R.
Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing Erf1-Erf3 or Erf1-Abce1.
Cell Rep., 8:59-, 2014

PubMed Abstract: Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP hydrolysis, eRF3 dissociates, and ABCE1 can bind to eRF1-loaded ribosomes to stimulate peptide release and ribosomal subunit dissociation. Here, we present cryoelectron microscopic (cryo-EM) structures of a pretermination complex containing eRF1-eRF3 and a termination/prerecycling complex containing eRF1-ABCE1. eRF1 undergoes drastic conformational changes: its central domain harboring the catalytically important GGQ loop is either packed against eRF3 or swung toward the peptidyl transferase center when bound to ABCE1. Additionally, in complex with eRF3, the N-terminal domain of eRF1 positions the conserved NIKS motif proximal to the stop codon, supporting its suggested role in decoding, yet it appears to be delocalized in the presence of ABCE1. These results suggest that stop codon decoding and peptide release can be uncoupled during termination.

PubMed: 25001285
DOI: 10.1016/J.CELREP.2014.04.058

実験手法

ELECTRON MICROSCOPY (9.1 Å)