Evidence map›Paper›PMID 12093756›Full record

ArticleThe EMBO journal2002

Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process.

Mikel Valle, Jayati Sengupta, Neil K Swami, Robert A Grassucci, Nils Burkhardt, Knud H Nierhaus, Rajendra K Agrawal, Joachim Frank

Abstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
–field-weighted citation impact
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

124 citing papers in PubMed.

  1. 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
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Joachim Frank's Binding with the Ribosome.Structure (London, England : 1993) · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. The translation elongation cycle-capturing multiple states by cryo-electron microscopy.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review

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

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Mikel ValleHoward Hughes Medical Institute, Health Research, Inc., Empire State Plaza, Albany, NY 12201-0509, USA.
Jayati Sengupta
Neil K Swami
Robert A Grassucci
Nils Burkhardt
Knud H Nierhaus
Rajendra K Agrawal
Joachim Frank

Funding

ZERNIKE PHASE-CONTRAST IMAGINGP41RR001219 · NCRR · WADSWORTH CENTER · PI MANNELLA, CARMEN A. · 1985 to 2010
$11.1M
Structural Aspects of Protein Synthesis in the Mammalian MitochondriaR01GM061576 · NIGMS · WADSWORTH CENTER · PI AGRAWAL, RAJENDRA K · 2001 to 2018
$6.4M
Time-resolved Cryo-EM of Short-lived States in Eukaryotic TranslationR01GM055440 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2020
$5.1M
STRUCTURAL ANALYSIS OF MACROMOLECULAR ASSEMBLYR37GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2006
$2.8M
NCRR NIH HHS P41 RR001219NCRR NIH HHS P41 RR01219NIGMS NIH HHS R01 GM055440NIGMS NIH HHS R01 GM061576NIGMS NIH HHS R01 GM55440NIGMS NIH HHS R01 GM61576NIGMS NIH HHS R37 GM029169NIGMS NIH HHS R37 GM29169
6 · The paper itself

Abstract

During the elongation cycle of protein biosynthesis, the specific amino acid coded for by the mRNA is delivered by a complex that is comprised of the cognate aminoacyl-tRNA, elongation factor Tu and GTP. As this ternary complex binds to the ribosome, the anticodon end of the tRNA reaches the decoding center in the 30S subunit. Here we present the cryo- electron microscopy (EM) study of an Escherichia coli 70S ribosome-bound ternary complex stalled with an antibiotic, kirromycin. In the cryo-EM map the anticodon arm of the tRNA presents a new conformation that appears to facilitate the initial codon-anticodon interaction. Furthermore, the elbow region of the tRNA is seen to contact the GTPase-associated center on the 50S subunit of the ribosome, suggesting an active role of the tRNA in the transmission of the signal prompting the GTP hydrolysis upon codon recognition.

Indexed as

Cryoelectron MicroscopyPeptide Chain Elongation, TranslationalAnticodonCodonEscherichia coliEscherichia coli ProteinsGuanosine DiphosphateGuanosine TriphosphateImage Processing, Computer-AssistedMacromolecular SubstancesModels, MolecularNucleic Acid ConformationPeptide Elongation Factor TuProtein ConformationPyridonesRibosomesAnticodonCodonEscherichia coli ProteinsGuanosine DiphosphateGuanosine TriphosphateMacromolecular SubstancesmocimycinPeptide Elongation Factor TuPyridonesRNA, TransferRNA, Transfer, Amino AcylRNA, Transfer, Phe

Identifiers

PMID12093756
PMCPMC126079

What OpenQuestion holds

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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.