3E1Y

Crystal structure of human eRF1/eRF3 complex

3E1Y の概要

• エントリーDOI: 10.2210/pdb3e1y/pdb
• 関連するPDBエントリー: 3E20
• 分子名称: Eukaryotic peptide chain release factor subunit 1, Eukaryotic peptide chain release factor GTP-binding subunit ERF3A, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: translation termination, erf1, erf3, peptide release, ptc, protein biosynthesis, gtp-binding, nucleotide-binding, translation
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm: P62495
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 294134.35

構造登録者

Cheng, Z.,Lim, M.,Kong, C.,Song, H. (登録日: 2008-08-05, 公開日: 2009-05-19, 最終更新日: 2024-10-16)

主引用文献

Cheng, Z.,Saito, K.,Pisarev, A.V.,Wada, M.,Pisareva, V.P.,Pestova, T.V.,Gajda, M.,Round, A.,Kong, C.,Lim, M.,Nakamura, Y.,Svergun, D.I.,Ito, K.,Song, H.
Structural insights into eRF3 and stop codon recognition by eRF1
Genes Dev., 23:1106-1118, 2009

PubMed Abstract: Eukaryotic translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act cooperatively to ensure efficient stop codon recognition and fast polypeptide release. The crystal structures of human and Schizosaccharomyces pombe full-length eRF1 in complex with eRF3 lacking the GTPase domain revealed details of the interaction between these two factors and marked conformational changes in eRF1 that occur upon binding to eRF3, leading eRF1 to resemble a tRNA molecule. Small-angle X-ray scattering analysis of the eRF1/eRF3/GTP complex suggested that eRF1's M domain contacts eRF3's GTPase domain. Consistently, mutation of Arg192, which is predicted to come in close contact with the switch regions of eRF3, revealed its important role for eRF1's stimulatory effect on eRF3's GTPase activity. An ATP molecule used as a crystallization additive was bound in eRF1's putative decoding area. Mutational analysis of the ATP-binding site shed light on the mechanism of stop codon recognition by eRF1.

PubMed: 19417105
DOI: 10.1101/gad.1770109

実験手法

X-RAY DIFFRACTION (3.8 Å)