Evidence map›Paper›PMID 23769667›Full record

ArticleStructure (London, England : 1993)2013

Crystal structure of the 70S ribosome bound with the Q253P mutant form of release factor RF2.

Natalia Santos, Jianyu Zhu, John Paul Donohue, Andrei A Korostelev, Harry F Noller

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Review
  4. Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  10. Review
  11. Article
  12. Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

5 authors at 2 institutions in 1 country.

Natalia SantosCenter for Molecular Biology of RNA and Department of Molecular, Cell and Developmental Biology, University of California at Santa Cruz, Santa Cruz, CA 95064, USA.
Jianyu Zhu
John Paul Donohue
Andrei A Korostelev
Harry F Noller
University of California, Santa Cruz · USUniversity of Massachusetts Chan Medical School · US

Funding

CRYSTAL STRUCTURE OF THE RIBOSOMER01GM059140 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1999 to 2015
$7.2M
RIBOSOME STRUCTURE AND FUNCTIONR01GM017129 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 1985 to 2015
$6.9M
MINOS (Macromolecular Insights on Nucleic acids Optimized by Scattering)R01GM105404 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 2012 to 2015
$2.1M
A High-Throughput Crystallization Screening System for the UCSC Macromolecular X-S10RR024611 · NCRR · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI NOLLER, HARRY F · 2008 to 2008
$250k
NCRR NIH HHS S10 RR024611NIGMS NIH HHS R01 GM017129NIGMS NIH HHS R01 GM059140NIGMS NIH HHS R01 GM105404
6 · The paper itself

Abstract

Bacterial translation termination is mediated by release factors RF1 and RF2, which recognize stop codons and catalyze hydrolysis of the peptidyl-tRNA ester bond. The catalytic mechanism has been debated. We proposed that the backbone amide NH group, rather than the side chain, of the glutamine of the universally conserved GGQ motif participates in catalysis by H-bonding to the tetrahedral transition-state intermediate and by product stabilization. This was supported by complete loss of RF1 catalytic activity when glutamine is replaced by proline, the only residue that lacks a backbone NH group. Here, we present the 3.4 Å crystal structure of the ribosome complex containing the RF2 Q253P mutant and find that its fold, including the GGP sequence, is virtually identical to that of wild-type RF2. This rules out proline-induced misfolding and further supports the proposal that catalytic activity requires interaction of the Gln-253 backbone amide with the 3' end of peptidyl-tRNA.

Indexed as

Thermus thermophilusBacterial ProteinsCrystallography, X-RayModels, MolecularMutation, MissenseNucleic Acid ConformationPeptide Termination FactorsProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialRNA, BacterialRNA, RibosomalBacterial Proteinspeptide chain termination release factor 2Peptide Termination FactorsRNA, BacterialRNA, Ribosomal

Identifiers

PMID23769667
PMCPMC3923520
OpenAlexW2147981074

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.