6FBZ

Crystal structure of the eIF4E-eIF4G complex from Chaetomium thermophilum in the cap-bound state

6FBZ の概要

• エントリーDOI: 10.2210/pdb6fbz/pdb
• 分子名称: Eukaryotic translation initiation factor 4E-like protein,Eukaryotic translation initiation factor 4E-like protein, Eukaryotic translation initiation factor 4G, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: translation translational control translation initiation gene expression, translation
• 由来する生物種: Chaetomium thermophilum var. thermophilum DSM 1495; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32667.84

構造登録者

Gruener, S.,Valkov, E. (登録日: 2017-12-20, 公開日: 2018-06-27, 最終更新日: 2024-01-17)

主引用文献

Gruner, S.,Weber, R.,Peter, D.,Chung, M.Y.,Igreja, C.,Valkov, E.,Izaurralde, E.
Structural motifs in eIF4G and 4E-BPs modulate their binding to eIF4E to regulate translation initiation in yeast.
Nucleic Acids Res., 46:6893-6908, 2018

PubMed Abstract: The interaction of the eukaryotic initiation factor 4G (eIF4G) with the cap-binding protein eIF4E initiates cap-dependent translation and is regulated by the 4E-binding proteins (4E-BPs), which compete with eIF4G to repress translation. Metazoan eIF4G and 4E-BPs interact with eIF4E via canonical and non-canonical motifs that bind to the dorsal and lateral surface of eIF4E in a bipartite recognition mode. However, previous studies pointed to mechanistic differences in how fungi and metazoans regulate protein synthesis. We present crystal structures of the yeast eIF4E bound to two yeast 4E-BPs, p20 and Eap1p, as well as crystal structures of a fungal eIF4E-eIF4G complex. We demonstrate that the core principles of molecular recognition of eIF4E are in fact highly conserved among translational activators and repressors in eukaryotes. Finally, we reveal that highly specialized structural motifs do exist and serve to modulate the affinity of protein-protein interactions that regulate cap-dependent translation initiation in fungi.

PubMed: 30053226
DOI: 10.1093/nar/gky542

実験手法

X-RAY DIFFRACTION (1.496 Å)