6I7T

eIF2B:eIF2 complex

Summary for 6I7T

• Entry DOI: 10.2210/pdb6i7t/pdb
• Related: 6I3M
• EMDB information: 4404 4428
• Descriptor: Translation initiation factor eIF-2B subunit alpha, Translation initiation factor eIF-2B subunit delta, Translation initiation factor eIF-2B subunit beta, ... (8 entities in total)
• Functional Keywords: translational control eif2 integrated stress response eif2b translation, translation
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 16
• Total formula weight: 837967.41

Authors

Adomavicius, T.,Guaita, M.,Roseman, A.M.,Pavitt, G.D. (deposition date: 2018-11-17, release date: 2019-05-22, Last modification date: 2024-05-15)

Primary citation

Adomavicius, T.,Guaita, M.,Zhou, Y.,Jennings, M.D.,Latif, Z.,Roseman, A.M.,Pavitt, G.D.
The structural basis of translational control by eIF2 phosphorylation.
Nat Commun, 10:2136-2136, 2019

PubMed Abstract: Protein synthesis in eukaryotes is controlled by signals and stresses via a common pathway, called the integrated stress response (ISR). Phosphorylation of the translation initiation factor eIF2 alpha at a conserved serine residue mediates translational control at the ISR core. To provide insight into the mechanism of translational control we have determined the structures of eIF2 both in phosphorylated and unphosphorylated forms bound with its nucleotide exchange factor eIF2B by electron cryomicroscopy. The structures reveal that eIF2 undergoes large rearrangements to promote binding of eIF2α to the regulatory core of eIF2B comprised of the eIF2B alpha, beta and delta subunits. Only minor differences are observed between eIF2 and eIF2αP binding to eIF2B, suggesting that the higher affinity of eIF2αP for eIF2B drives translational control. We present a model for controlled nucleotide exchange and initiator tRNA binding to the eIF2/eIF2B complex.

PubMed: 31086188
DOI: 10.1038/s41467-019-10167-3

Experimental method

ELECTRON MICROSCOPY (4.61 Å)