Evidence map›Paper›PMID 23527033›Full record

ArticlePloS one2013

Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex.

Shu Feng, Yun Chen, Yong-Gui Gao

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  6. The GTPase BipA expressed at low temperature inThe Journal of biological chemistry · 2018
    Article
  7. Review
  8. Article
  9. Review
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  11. Model of the pathway of -1 frameshifting: Kinetics.Biochemistry and biophysics reports · 2016
    Article
  12. Structure of BipA in GTP form bound to the ratcheted ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 2 countries.

Shu FengSchool of Biological Science, Nanyang Technological University, Singapore.
Yun Chen
Yong-Gui Gao
Nanyang Technological University · SGMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council U105184332
6 · The paper itself

Abstract

During the translation cycle, a cognate deacylated tRNA can only move together with the codon into the E site. We here present the first structure of a cognate tRNA bound to the ribosomal E site resulting from translocation by EF-G, in which an entire L1 stalk (L1 protein and L1 rRNA) interacts with E-site tRNA (E-tRNA), representing an authentic ribosome elongation complex. Our results revealed that the Watson-Crick base pairing is formed at the first and second codon-anticodon positions in the E site in the ribosome elongation complex, whereas the codon-anticodon interaction in the third position is indirect. Analysis of the observed conformations of mRNA and E-tRNA suggests that the ribosome intrinsically has the potential to form codon-anticodon interaction in the E site, independently of the mRNA configuration. We also present a detailed description of the biologically relevant position of the entire L1 stalk and its interacting cognate E-tRNA, which provides a better understanding of the structural basis for translation elongation. Furthermore, to gain insight into translocation, we report the positioning of protein L6 contacting EF-G, as well as the conformational change of the C-terminal tail of protein S13 in the decoding center.

Indexed as

CodonModels, MolecularMultiprotein ComplexesNucleic Acid ConformationPeptide Chain Elongation, TranslationalPeptide Elongation FactorsProtein BindingProtein ConformationRibosome SubunitsRNA, MessengerRNA, TransferCodonMultiprotein ComplexesPeptide Elongation FactorsRNA, MessengerRNA, Transfer

Identifiers

PMID23527033
PMCPMC3602588
OpenAlexW2013106129

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.