Evidence map›Paper›PMID 19833920›Full record

ArticleScience (New York, N.Y.)2009

The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA.

T Martin Schmeing, Rebecca M Voorhees, Ann C Kelley, Yong-Gui Gao, Frank V Murphy, John R Weir, V Ramakrishnan

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 298 papers.

0numbers the graph read from it
0cells of the map it votes in
298citing papers in PubMed
22.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

298 citing papers in PubMed, 542 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. HflX-mediated drug resistance through ribosome splitting and rRNA disordering in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Single-Molecule Studies of Cognate and Near-Cognate Elongation in anbioRxiv : the preprint server for biology · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024
    Review
  20. Tuning tRNAs for improved translation.Frontiers in genetics · 2024
    Review

238 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

T Martin Schmeing *MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Rebecca M Voorhees *MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Ann C KelleyMRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Yong-Gui GaoMRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Frank V MurphyMRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
John R WeirMRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
V RamakrishnanMRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184332Wellcome Trust 082086
6 · The paper itself

Abstract

The ribosome selects a correct transfer RNA (tRNA) for each amino acid added to the polypeptide chain, as directed by messenger RNA. Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. The signaling pathway that leads to GTP hydrolysis upon codon recognition is critical to accurate decoding. Here we present the crystal structure of the ribosome complexed with EF-Tu and aminoacyl-tRNA, refined to 3.6 angstrom resolution. The structure reveals details of the tRNA distortion that allows aminoacyl-tRNA to interact simultaneously with the decoding center of the 30S subunit and EF-Tu at the factor binding site. A series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathway between the decoding center and the guanosine triphosphatase center of EF-Tu.

Indexed as

Crystallography, X-RayEnzyme ActivationGenetic CodeGTP PhosphohydrolasesModels, MolecularNucleic Acid ConformationPeptide Elongation Factor TuProtein BindingProtein ConformationProtein Structure, TertiaryRibosomesRNA, BacterialRNA, Transfer, Amino AcylRNA, Transfer, PheRNA, Transfer, ThrThermus thermophilusGTP PhosphohydrolasesPeptide Elongation Factor TuRNA, BacterialRNA, Transfer, Amino AcylRNA, Transfer, PheRNA, Transfer, Thr

Identifiers

PMID19833920
PMCPMC3763470
OpenAlexW2142672816

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.