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7O7Z

Rabbit 80S ribosome stalled close to the mutated SARS-CoV-2 slippery site by a pseudoknot (classified for pseudoknot)

This is a non-PDB format compatible entry.
Summary for 7O7Z
Entry DOI10.2210/pdb7o7z/pdb
EMDB information12757
Descriptor18S rRNA, E-site tRNA, P-site Phe-tRNA(Phe), ... (92 entities in total)
Functional Keywordsframeshift, virus, pseudoknot, ribosome
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
More
Total number of polymer chains86
Total formula weight4071783.04
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 citationBhatt, 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: 34029205
DOI: 10.1126/science.abf3546
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.4 Å)
Structure validation

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