Evidence map›Paper›PMID 31873307›Full record

ArticleNature structural & molecular biology2020

Structural basis for ribosome recycling by RRF and tRNA.

Dejian Zhou, Takehito Tanzawa, Jinzhong Lin, Matthieu G Gagnon

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  6. The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024
    Review
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  17. Novel tigecycline resistance mechanisms inEmerging microbes & infections · 2021
    Article
  18. Article
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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

4 authors at 2 institutions in 2 countries.

Dejian Zhou *State Key Laboratory of Genetic Engineering, School of Life Sciences, Zhongshan Hospital, Fudan University, Shanghai, China.ORCID http://orcid.org/0000-0002-4743-6077
Takehito Tanzawa *Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Jinzhong LinState Key Laboratory of Genetic Engineering, School of Life Sciences, Zhongshan Hospital, Fudan University, Shanghai, China. linjinzhong@fudan.edu.cn.ORCID http://orcid.org/0000-0001-5666-8526
Matthieu G GagnonDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA. magagnon@utmb.edu.ORCID http://orcid.org/0000-0003-4516-604X
Fudan University · CNThe University of Texas Medical Branch at Galveston · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

The bacterial ribosome is recycled into subunits by two conserved proteins, elongation factor G (EF-G) and the ribosome recycling factor (RRF). The molecular basis for ribosome recycling by RRF and EF-G remains unclear. Here, we report the crystal structure of a posttermination Thermus thermophilus 70S ribosome complexed with EF-G, RRF and two transfer RNAs at a resolution of 3.5 Å. The deacylated tRNA in the peptidyl (P) site moves into a previously unsuspected state of binding (peptidyl/recycling, p/R) that is analogous to that seen during initiation. The terminal end of the p/R-tRNA forms nonfavorable contacts with the 50S subunit while RRF wedges next to central inter-subunit bridges, illuminating the active roles of tRNA and RRF in dissociation of ribosomal subunits. The structure uncovers a missing snapshot of tRNA as it transits between the P and exit (E) sites, providing insights into the mechanisms of ribosome recycling and tRNA translocation.

Indexed as

Bacterial ProteinsCrystallography, X-RayModels, MolecularPeptide Elongation Factor GProtein ConformationRibosomal ProteinsRibosomesRibosome Subunits, Large, BacterialRNA, TransferThermus thermophilusBacterial ProteinsPeptide Elongation Factor GRibosomal Proteinsribosome releasing factorRNA, Transfer

Identifiers

PMID31873307
PMCPMC9150878
OpenAlexW2996325830

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.