6O85
Electron cryo-microscopy of the eukaryotic translation initiation factor 2B bound to eukaryotic translation initiation factor 2 from Homo sapiens
Summary for 6O85
| Entry DOI | 10.2210/pdb6o85/pdb |
| EMDB information | 0651 |
| Descriptor | 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) |
| Functional Keywords | eukaryotic translation initiation factor 2b, eukaryotic translation initiation factor 2, translation |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 13 |
| Total formula weight | 615216.68 |
| Authors | Nguyen, H.C.,Kenner, L.R.,Frost, A.S. (deposition date: 2019-03-08, release date: 2019-05-15, Last modification date: 2024-03-13) |
| Primary citation | 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 Cited by 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: 31048491DOI: 10.1126/science.aaw2922 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.03 Å) |
Structure validation
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