7O80
Rabbit 80S ribosome in complex with eRF1 and ABCE1 stalled at the STOP codon in the mutated SARS-CoV-2 slippery site
This is a non-PDB format compatible entry.
Summary for 7O80
| Entry DOI | 10.2210/pdb7o80/pdb |
| EMDB information | 12758 |
| Descriptor | 18S rRNA, E-site tRNA, P-site Leu-tRNA(Leu), ... (95 entities in total) |
| Functional Keywords | frameshift, virus, pseudoknot, ribosome |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) More |
| Total number of polymer chains | 88 |
| Total formula weight | 4156661.93 |
| Authors | Bhatt, P.R.,Scaiola, A.,Leibundgut, M.A.,Atkins, J.F.,Ban, N. (deposition date: 2021-04-14, release date: 2021-06-02, Last modification date: 2024-04-24) |
| Primary citation | Bhatt, P.R.,Scaiola, A.,Loughran, G.,Leibundgut, M.,Kratzel, A.,Meurs, R.,Dreos, R.,O'Connor, K.M.,McMillan, A.,Bode, J.W.,Thiel, V.,Gatfield, D.,Atkins, J.F.,Ban, N. Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome. Science, 372:1306-1313, 2021 Cited by PubMed Abstract: Programmed ribosomal frameshifting is a key event during translation of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) RNA genome that allows synthesis of the viral RNA-dependent RNA polymerase and downstream proteins. Here, we present the cryo-electron microscopy structure of a translating mammalian ribosome primed for frameshifting on the viral RNA. The viral RNA adopts a pseudoknot structure that lodges at the entry to the ribosomal messenger RNA (mRNA) channel to generate tension in the mRNA and promote frameshifting, whereas the nascent viral polyprotein forms distinct interactions with the ribosomal tunnel. Biochemical experiments validate the structural observations and reveal mechanistic and regulatory features that influence frameshifting efficiency. Finally, we compare compounds previously shown to reduce frameshifting with respect to their ability to inhibit SARS-CoV-2 replication, establishing coronavirus frameshifting as a target for antiviral intervention. PubMed: 34029205DOI: 10.1126/science.abf3546 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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