6IP5
Cryo-EM structure of the CMV-stalled human 80S ribosome (Structure ii)
This is a non-PDB format compatible entry.
Summary for 6IP5
| Entry DOI | 10.2210/pdb6ip5/pdb |
| EMDB information | 9699 9701 9702 9703 9704 |
| Descriptor | 28S ribosomal RNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (83 entities in total) |
| Functional Keywords | ribosome, translation |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 84 |
| Total formula weight | 3857099.05 |
| Authors | Yokoyama, T.,Shigematsu, H.,Shirouzu, M.,Imataka, H.,Ito, T. (deposition date: 2018-11-02, release date: 2019-05-29, Last modification date: 2019-11-06) |
| Primary citation | Yokoyama, T.,Machida, K.,Iwasaki, W.,Shigeta, T.,Nishimoto, M.,Takahashi, M.,Sakamoto, A.,Yonemochi, M.,Harada, Y.,Shigematsu, H.,Shirouzu, M.,Tadakuma, H.,Imataka, H.,Ito, T. HCV IRES Captures an Actively Translating 80S Ribosome. Mol.Cell, 74:1205-1214.e8, 2019 Cited by PubMed Abstract: Translation initiation of hepatitis C virus (HCV) genomic RNA is induced by an internal ribosome entry site (IRES). Our cryoelectron microscopy (cryo-EM) analysis revealed that the HCV IRES binds to the solvent side of the 40S platform of the cap-dependently translating 80S ribosome. Furthermore, we obtained the cryo-EM structures of the HCV IRES capturing the 40S subunit of the IRES-dependently translating 80S ribosome. In the elucidated structures, the HCV IRES "body," consisting of domain III except for subdomain IIIb, binds to the 40S subunit, while the "long arm," consisting of domain II, remains flexible and does not impede the ongoing translation. Biochemical experiments revealed that the cap-dependently translating ribosome becomes a better substrate for the HCV IRES than the free ribosome. Therefore, the HCV IRES is likely to efficiently induce the translation initiation of its downstream mRNA with the captured translating ribosome as soon as the ongoing translation terminates. PubMed: 31080011DOI: 10.1016/j.molcel.2019.04.022 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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