8HUJ
Cryo-EM structure of the J-K-St region of EMCV IRES in complex with eIF4G-HEAT1 and eIF4A
Summary for 8HUJ
| Entry DOI | 10.2210/pdb8huj/pdb |
| EMDB information | 35041 |
| Descriptor | Eukaryotic initiation factor 4A-I, Eukaryotic translation initiation factor 4 gamma 1, IRES RNA (J-K-St), ... (5 entities in total) |
| Functional Keywords | translation initiation factors, translation, rna binding protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 115357.77 |
| Authors | Suzuki, H.,Fujiyoshi, Y.,Imai, S.,Shimada, I. (deposition date: 2022-12-24, release date: 2023-08-02, Last modification date: 2023-09-13) |
| Primary citation | Imai, S.,Suzuki, H.,Fujiyoshi, Y.,Shimada, I. Dynamically regulated two-site interaction of viral RNA to capture host translation initiation factor. Nat Commun, 14:4977-4977, 2023 Cited by PubMed Abstract: Many RNA viruses employ internal ribosome entry sites (IRESs) in their genomic RNA to commandeer the host's translational machinery for replication. The IRES from encephalomyocarditis virus (EMCV) interacts with eukaryotic translation initiation factor 4 G (eIF4G), recruiting the ribosomal subunit for translation. Here, we analyze the three-dimensional structure of the complex composed of EMCV IRES, the HEAT1 domain fragment of eIF4G, and eIF4A, by cryo-electron microscopy. Two distinct eIF4G-interacting domains on the IRES are identified, and complex formation changes the angle therebetween. Further, we explore the dynamics of these domains by using solution NMR spectroscopy, revealing conformational equilibria in the microsecond to millisecond timescale. In the lowly-populated conformations, the base-pairing register of one domain is shifted with the structural transition of the three-way junction, as in the complex structure. Our study provides insights into the viral RNA's sophisticated strategy for optimal docking to hijack the host protein. PubMed: 37640715DOI: 10.1038/s41467-023-40582-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.76 Å) |
Structure validation
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