3WBK

crystal structure analysis of eukaryotic translation initiation factor 5B and 1A complex

3WBK の概要

• エントリーDOI: 10.2210/pdb3wbk/pdb
• 関連するPDBエントリー: 3WBI 3WBJ
• 分子名称: Eukaryotic translation initiation factor 5B, Eukaryotic translation initiation factor 1A (2 entities in total)
• 機能のキーワード: flexible, eukaryotic translation initiation, biosynthetic protein
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Cytoplasm : P39730
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 150488.39

構造登録者

Zheng, A.,Yamamoto, R.,Ose, T.,Yu, J.,Tanaka, I.,Yao, M. (登録日: 2013-05-20, 公開日: 2014-11-19, 最終更新日: 2023-11-08)

主引用文献

Zheng, A.,Yu, J.,Yamamoto, R.,Ose, T.,Tanaka, I.,Yao, M.
X-ray structures of eIF5B and the eIF5B-eIF1A complex: the conformational flexibility of eIF5B is restricted on the ribosome by interaction with eIF1A
Acta Crystallogr.,Sect.D, 70:3090-3098, 2014

PubMed Abstract: eIF5B and eIF1A are two translation-initiation factors that are universally conserved among all kingdoms. They show a unique interaction in eukaryotes which is important for ribosomal subunit joining. Here, the structures of two isolated forms of yeast eIF5B and of the eIF5B-eIF1A complex (eIF1A and eIF5B do not contain the respective N-terminal domains) are reported. The eIF5B-eIF1A structure shows that the C-terminal tail of eIF1A binds to eIF5B domain IV, while the core domain of eIF1A is invisible in the electron-density map. Although the individual domains in all structures of eIF5B or archaeal IF5B (aIF5B) are similar, their domain arrangements are significantly different, indicating high structural flexibility, which is advantageous for conformational change during ribosomal subunit joining. Based on these structures, models of eIF5B, eIF1A and tRNAi(Met) on the 80S ribosome were built. The models suggest that the interaction between the eIF1A C-terminal tail and eIF5B helps tRNAi(Met) to bind to eIF5B domain IV, thus preventing tRNAi(Met) dissociation, stabilizing the interface for subunit joining and providing a checkpoint for correct ribosome assembly.

PubMed: 25478828
DOI: 10.1107/S1399004714021476

実験手法

X-RAY DIFFRACTION (3.3 Å)