6QG1

Structure of eIF2B-eIF2 (phosphorylated at Ser51) complex (model 2)

Summary for 6QG1

• Entry DOI: 10.2210/pdb6qg1/pdb
• Related: 6QG0
• EMDB information: 4543 4544
• Descriptor: Translation initiation factor eIF-2B subunit alpha, Translation initiation factor eIF-2B subunit beta, Translation initiation factor eIF-2B subunit gamma, ... (8 entities in total)
• Functional Keywords: integrated stress response, isr, translation, initiation factors, phosphorylation, eif2, eif2b, trnai, gef, heat domain, eif2 alpha
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 16
• Total formula weight: 838127.37

Authors

Llacer, J.L.,Gordiyenko, Y.,Ramakrishnan, V. (deposition date: 2019-01-10, release date: 2019-06-26, Last modification date: 2019-12-18)

Primary citation

Gordiyenko, Y.,Llacer, J.L.,Ramakrishnan, V.
Structural basis for the inhibition of translation through eIF2 alpha phosphorylation.
Nat Commun, 10:2640-2640, 2019

PubMed Abstract: 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.

PubMed: 31201334
DOI: 10.1038/s41467-019-10606-1

Experimental method

ELECTRON MICROSCOPY (4.2 Å)