7LV0

Pre-translocation rotated ribosome +1-frameshifting(CCC-A) complex (Structure Irot-FS)

This is a non-PDB format compatible entry.

Summary for 7LV0

• Entry DOI: 10.2210/pdb7lv0/pdb
• EMDB information: 22669 22670 22671 22672 22673 22674 23528
• Descriptor: 50S ribosomal protein L2, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (60 entities in total)
• Functional Keywords: ribosome, ef-g, trna, translation
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 58
• Total formula weight: 2221062.46

Authors

Demo, G.,Loveland, A.B.,Svidritskiy, E.,Gamper, H.B.,Hou, Y.M.,Korostelev, A.A. (deposition date: 2021-02-23, release date: 2021-07-28, Last modification date: 2024-10-23)

Primary citation

Demo, G.,Gamper, H.B.,Loveland, A.B.,Masuda, I.,Carbone, C.E.,Svidritskiy, E.,Hou, Y.M.,Korostelev, A.A.
Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation.
Nat Commun, 12:4644-4644, 2021

PubMed Abstract: Frameshifting of mRNA during translation provides a strategy to expand the coding repertoire of cells and viruses. How and where in the elongation cycle +1-frameshifting occurs remains poorly understood. We describe seven ~3.5-Å-resolution cryo-EM structures of 70S ribosome complexes, allowing visualization of elongation and translocation by the GTPase elongation factor G (EF-G). Four structures with a + 1-frameshifting-prone mRNA reveal that frameshifting takes place during translocation of tRNA and mRNA. Prior to EF-G binding, the pre-translocation complex features an in-frame tRNA-mRNA pairing in the A site. In the partially translocated structure with EF-G•GDPCP, the tRNA shifts to the +1-frame near the P site, rendering the freed mRNA base to bulge between the P and E sites and to stack on the 16S rRNA nucleotide G926. The ribosome remains frameshifted in the nearly post-translocation state. Our findings demonstrate that the ribosome and EF-G cooperate to induce +1 frameshifting during tRNA-mRNA translocation.

PubMed: 34330903
DOI: 10.1038/s41467-021-24911-1

Experimental method

ELECTRON MICROSCOPY (3.2 Å)