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7K50

Pre-translocation non-frameshifting(CCA-A) complex (Structure I)

This is a non-PDB format compatible entry.
Summary for 7K50
Entry DOI10.2210/pdb7k50/pdb
EMDB information22669 22670 22671 22672 22673 22674
Descriptor50S ribosomal protein L2, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (59 entities in total)
Functional Keywordsribosome, trna, translation
Biological sourceEscherichia coli K-12
More
Total number of polymer chains59
Total formula weight2245774.14
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 citationDemo, 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: 34330903
DOI: 10.1038/s41467-021-24911-1
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

227111

数据于2024-11-06公开中

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