7K50
Pre-translocation non-frameshifting(CCA-A) complex (Structure I)
This is a non-PDB format compatible entry.
Summary for 7K50
Entry DOI | 10.2210/pdb7k50/pdb |
EMDB information | 22669 22670 22671 22672 22673 22674 |
Descriptor | 50S ribosomal protein L2, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (59 entities in total) |
Functional Keywords | ribosome, trna, translation |
Biological source | Escherichia coli K-12 More |
Total number of polymer chains | 59 |
Total formula weight | 2245774.14 |
Authors | Demo, G.,Loveland, A.B.,Svidritskiy, E.,Gamper, H.B.,Hou, Y.M.,Korostelev, A.A. (deposition date: 2020-09-16, release date: 2021-07-28, Last modification date: 2024-05-29) |
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 Cited by 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: 34330903DOI: 10.1038/s41467-021-24911-1 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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