Evidence map›Paper›PMID 21051640›Full record

ArticleScience (New York, N.Y.)2010

The mechanism for activation of GTP hydrolysis on the ribosome.

Rebecca M Voorhees, T Martin Schmeing, Ann C Kelley, V Ramakrishnan

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 221 papers.

0numbers the graph read from it
0cells of the map it votes in
221citing papers in PubMed
16.8field-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

221 citing papers in PubMed, 361 citations in OpenAlex.

  1. Review
  2. Article
  3. D81 Mutants Reveal Hidden EF-Tu Diversity while Natural Sequences Preserve Aspartate.Computational and structural biotechnology journal · 2026
    Article
  4. Article
  5. Article
  6. Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
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  11. Article
  12. Article
  13. Article
  14. Biomolecular NMR assignments · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Rebecca M Voorhees *MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
T Martin Schmeing *MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Ann C KelleyMRC 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

Protein synthesis requires several guanosine triphosphatase (GTPase) factors, including elongation factor Tu (EF-Tu), which delivers aminoacyl-transfer RNAs (tRNAs) to the ribosome. To understand how the ribosome triggers GTP hydrolysis in translational GTPases, we have determined the crystal structure of EF-Tu and aminoacyl-tRNA bound to the ribosome with a GTP analog, to 3.2 angstrom resolution. EF-Tu is in its active conformation, the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the γ-phosphate of GTP. This activated conformation is due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. The structure suggests a universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome.

Indexed as

Bacterial ProteinsCatalytic DomainCrystallography, X-RayEnzyme ActivationGuanosine TriphosphateHydrolysisHydrophobic and Hydrophilic InteractionsNucleic Acid ConformationParomomycinPeptide Elongation Factor TuPhosphatesProtein Structure, TertiaryRibosomesRNA, BacterialRNA, Ribosomal, 23SRNA, Transfer, Amino AcylBacterial Proteinsguanosine 5'-(beta,gamma-methylene)triphosphateGuanosine TriphosphateParomomycinPeptide Elongation Factor TuPhosphatesRNA, BacterialRNA, Ribosomal, 23SRNA, Transfer, Amino Acyl

Identifiers

PMID21051640
PMCPMC3763471
OpenAlexW2165048399

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.