6O81

Electron cryo-microscopy of the eukaryotic translation initiation factor 2B bound to translation initiation factor 2 from Homo sapiens

6O81 の概要

• エントリーDOI: 10.2210/pdb6o81/pdb
• EMDBエントリー: 0649
• 分子名称: Translation initiation factor eIF-2B subunit epsilon, Translation initiation factor eIF-2B subunit beta, Translation initiation factor eIF-2B subunit delta, ... (9 entities in total)
• 機能のキーワード: translation initiation, translation
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 703640.82

構造登録者

Nguyen, H.,Kenner, L.,Frost, A. (登録日: 2019-03-08, 公開日: 2019-05-15, 最終更新日: 2025-05-14)

主引用文献

Kenner, L.R.,Anand, A.A.,Nguyen, H.C.,Myasnikov, A.G.,Klose, C.J.,McGeever, L.A.,Tsai, J.C.,Miller-Vedam, L.E.,Walter, P.,Frost, A.
eIF2B-catalyzed nucleotide exchange and phosphoregulation by the integrated stress response.
Science, 364:491-495, 2019

PubMed Abstract: The integrated stress response (ISR) tunes the rate of protein synthesis. Control is exerted by phosphorylation of the general translation initiation factor eIF2. eIF2 is a guanosine triphosphatase that becomes activated by eIF2B, a two-fold symmetric and heterodecameric complex that functions as eIF2's dedicated nucleotide exchange factor. Phosphorylation converts eIF2 from a substrate into an inhibitor of eIF2B. We report cryo-electron microscopy structures of eIF2 bound to eIF2B in the dephosphorylated state. The structures reveal that the eIF2B decamer is a static platform upon which one or two flexible eIF2 trimers bind and align with eIF2B's bipartite catalytic centers to catalyze nucleotide exchange. Phosphorylation refolds eIF2α, allowing it to contact eIF2B at a different interface and, we surmise, thereby sequestering it into a nonproductive complex.

PubMed: 31048491
DOI: 10.1126/science.aaw2922

実験手法

ELECTRON MICROSCOPY (3.21 Å)