+検索条件
-Structure paper
タイトル | Structural basis for the inhibition of translation through eIF2α phosphorylation. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 2640, Year 2019 |
掲載日 | 2019年6月14日 |
著者 | Yuliya Gordiyenko / José Luis Llácer / V Ramakrishnan / |
PubMed 要旨 | One of the responses to stress by eukaryotic cells is the down-regulation of protein synthesis by phosphorylation of translation initiation factor eIF2. Phosphorylation results in low availability of ...One of the responses to stress by eukaryotic cells is the down-regulation of protein synthesis by phosphorylation of translation initiation factor eIF2. Phosphorylation results in low availability of the eIF2 ternary complex (eIF2-GTP-tRNAi) by affecting the interaction of eIF2 with its GTP-GDP exchange factor eIF2B. We have determined the cryo-EM structure of yeast eIF2B in complex with phosphorylated eIF2 at an overall resolution of 4.2 Å. Two eIF2 molecules bind opposite sides of an eIF2B hetero-decamer through eIF2α-D1, which contains the phosphorylated Ser51. eIF2α-D1 is mainly inserted between the N-terminal helix bundle domains of δ and α subunits of eIF2B. Phosphorylation of Ser51 enhances binding to eIF2B through direct interactions of phosphate groups with residues in eIF2Bα and indirectly by inducing contacts of eIF2α helix 58-63 with eIF2Bδ leading to a competition with Met-tRNA. |
リンク | Nat Commun / PubMed:31201334 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.15 - 10.4 Å |
構造データ | EMDB-4543: Structure of eIF2B-eIF2 (phosphorylated at Ser51) complex (map 1) EMDB-4544: Structure of eIF2B-eIF2 (phosphorylated at Ser51) complex (map 2) EMDB-4545: Structure of eIF2B-eIF2 (phosphorylated at Ser51) complex (map A) EMDB-4546: Structure of eIF2B-eIF2 (phosphorylated at Ser51) complex (map B) |
由来 |
|
キーワード | TRANSLATION / integrated stress response / ISR / initiation factors / phosphorylation / eIF2 / eIF2B / tRNAi / GEF / heat domain / eIF2 alpha |