Summary for 6K72
| Entry DOI | 10.2210/pdb6k72/pdb |
| EMDB information | 9841 |
| 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 | translation initiation, translation |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 14 |
| Total formula weight | 684364.65 |
| Authors | Kashiwagi, K.,Yokoyama, T.,Ito, T. (deposition date: 2019-06-05, release date: 2019-07-10, Last modification date: 2024-03-27) |
| Primary citation | Kashiwagi, K.,Yokoyama, T.,Nishimoto, M.,Takahashi, M.,Sakamoto, A.,Yonemochi, M.,Shirouzu, M.,Ito, T. Structural basis for eIF2B inhibition in integrated stress response. Science, 364:495-499, 2019 Cited by PubMed Abstract: A core event in the integrated stress response, an adaptive pathway common to all eukaryotic cells in response to various stress stimuli, is the phosphorylation of eukaryotic translation initiation factor 2 (eIF2). Normally, unphosphorylated eIF2 transfers the methionylated initiator tRNA to the ribosome in a guanosine 5'-triphosphate-dependent manner. By contrast, phosphorylated eIF2 inhibits its specific guanine nucleotide exchange factor, eIF2B. To elucidate how the eIF2 phosphorylation status regulates the eIF2B activity, we determined cryo-electron microscopic and crystallographic structures of eIF2B in complex with unphosphorylated or phosphorylated eIF2. The unphosphorylated and phosphorylated forms of eIF2 bind to eIF2B in completely different manners: the nucleotide exchange-active and -inactive modes, respectively. These structures explain how phosphorylated eIF2 dominantly inhibits the nucleotide exchange activity of eIF2B. PubMed: 31048492DOI: 10.1126/science.aaw4104 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.6 Å) |
Structure validation
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