6D90
Mammalian 80S ribosome with a double translocated CrPV-IRES, P-site tRNA and eRF1.
This is a non-PDB format compatible entry.
Summary for 6D90
Entry DOI | 10.2210/pdb6d90/pdb |
EMDB information | 7834 |
Descriptor | Ribosomal protein L8, Ribosomal protein L11, eL13, ... (85 entities in total) |
Functional Keywords | ribosome, mammalian, crpv ires |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 85 |
Total formula weight | 3465649.22 |
Authors | Pisareva, V.P.,Pisarev, A.V.,Fernandez, I.S. (deposition date: 2018-04-27, release date: 2018-06-06, Last modification date: 2024-12-25) |
Primary citation | Pisareva, V.P.,Pisarev, A.V.,Fernandez, I.S. Dual tRNA mimicry in the Cricket Paralysis Virus IRES uncovers an unexpected similarity with the Hepatitis C Virus IRES. Elife, 7:-, 2018 Cited by PubMed Abstract: Co-opting the cellular machinery for protein production is a compulsory requirement for viruses. The Cricket Paralysis Virus employs an Internal Ribosomal Entry Site (CrPV-IRES) to express its structural genes in the late stage of infection. Ribosome hijacking is achieved by a sophisticated use of molecular mimicry to tRNA and mRNA, employed to manipulate intrinsically dynamic components of the ribosome. Binding and translocation through the ribosome is required for this IRES to initiate translation. We report two structures, solved by single particle electron cryo-microscopy (cryoEM), of a double translocated CrPV-IRES with aminoacyl-tRNA in the peptidyl site (P site) of the ribosome. CrPV-IRES adopts a previously unseen conformation, mimicking the acceptor stem of a canonical E site tRNA. The structures suggest a mechanism for the positioning of the first aminoacyl-tRNA shared with the distantly related Hepatitis C Virus IRES. PubMed: 29856316DOI: 10.7554/eLife.34062 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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