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5UYP

70S ribosome bound with near-cognate ternary complex base-paired to A site codon, open 30S (Structure II-nc)

This is a non-PDB format compatible entry.
Summary for 5UYP
Entry DOI10.2210/pdb5uyp/pdb
Related5UYK 5UYL 5UYM 5UYN 5UYQ
EMDB information8615 8616 8617 8618 8619 8620
Descriptor50S ribosomal protein L2, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (62 entities in total)
Functional Keywordsribosome, ef-tu, trna
Biological sourceEscherichia coli (strain K12)
More
Total number of polymer chains60
Total formula weight2288800.94
Authors
Loveland, A.B.,Demo, G.,Grigorieff, N.,Korostelev, A.A. (deposition date: 2017-02-24, release date: 2017-06-07, Last modification date: 2024-03-13)
Primary citationLoveland, A.B.,Demo, G.,Grigorieff, N.,Korostelev, A.A.
Ensemble cryo-EM elucidates the mechanism of translation fidelity
Nature, 546:113-117, 2017
Cited by
PubMed Abstract: Gene translation depends on accurate decoding of mRNA, the structural mechanism of which remains poorly understood. Ribosomes decode mRNA codons by selecting cognate aminoacyl-tRNAs delivered by elongation factor Tu (EF-Tu). Here we present high-resolution structural ensembles of ribosomes with cognate or near-cognate aminoacyl-tRNAs delivered by EF-Tu. Both cognate and near-cognate tRNA anticodons explore the aminoacyl-tRNA-binding site (A site) of an open 30S subunit, while inactive EF-Tu is separated from the 50S subunit. A transient conformation of decoding-centre nucleotide G530 stabilizes the cognate codon-anticodon helix, initiating step-wise 'latching' of the decoding centre. The resulting closure of the 30S subunit docks EF-Tu at the sarcin-ricin loop of the 50S subunit, activating EF-Tu for GTP hydrolysis and enabling accommodation of the aminoacyl-tRNA. By contrast, near-cognate complexes fail to induce the G530 latch, thus favouring open 30S pre-accommodation intermediates with inactive EF-Tu. This work reveals long-sought structural differences between the pre-accommodation of cognate and near-cognate tRNAs that elucidate the mechanism of accurate decoding.
PubMed: 28538735
DOI: 10.1038/nature22397
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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