Evidence map›Paper›PMID 28457609›Full record

ArticleCell2017

Cryo-EM Structure of a Relaxase Reveals the Molecular Basis of DNA Unwinding during Bacterial Conjugation.

Aravindan Ilangovan, Christopher W M Kay, Sandro Roier, Hassane El Mkami, Enrico Salvadori, Ellen L Zechner, Giulia Zanetti, Gabriel Waksman

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

38 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
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  8. Diversity and phage sensitivity to phages of porcine enterotoxigenicApplied and environmental microbiology · 2024
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  16. Structural basis for effector recognition by an antibacterial type IV secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

8 authors at 4 institutions in 2 countries.

Aravindan IlangovanInstitute of Structural and Molecular Biology, Birkbeck, Malet Street, London WC1E 7HX, UK.
Christopher W M KayInstitute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK; London Centre for Nanotechnology, University College London, 17-19 Gordon Street, London WC1H 0AH, UK.
Sandro RoierInstitute of Molecular Biosciences, University of Graz, BioTechMed-Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Hassane El MkamiSchool of Physics and Astronomy, University of St Andrews, St Andrews KY16 9SS, UK.
Enrico SalvadoriInstitute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK; London Centre for Nanotechnology, University College London, 17-19 Gordon Street, London WC1H 0AH, UK.
Ellen L ZechnerInstitute of Molecular Biosciences, University of Graz, BioTechMed-Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Giulia ZanettiInstitute of Structural and Molecular Biology, Birkbeck, Malet Street, London WC1E 7HX, UK. Electronic address: g.zanetti@mail.cryst.bbk.ac.uk.
Gabriel WaksmanInstitute of Structural and Molecular Biology, Birkbeck, Malet Street, London WC1E 7HX, UK; Institute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK. Electronic address: g.waksman@mail.cryst.bbk.ac.uk.
Institute of Structural and Molecular Biology · GBLondon Centre for Nanotechnology · GBUniversity of Graz · ATUniversity of St Andrews · GB

Funding

Wellcome Trust 098302Wellcome Trust 099149/Z/12/Z
6 · The paper itself

Abstract

Relaxases play essential roles in conjugation, the main process by which bacteria exchange genetic material, notably antibiotic resistance genes. They are bifunctional enzymes containing a trans-esterase activity, which is responsible for nicking the DNA strand to be transferred and for covalent attachment to the resulting 5'-phosphate end, and a helicase activity, which is responsible for unwinding the DNA while it is being transported to a recipient cell. Here we show that these two activities are carried out by two conformers that can both load simultaneously on the origin of transfer DNA. We solve the structure of one of these conformers by cryo electron microscopy to near-atomic resolution, elucidating the molecular basis of helicase function by relaxases and revealing insights into the mechanistic events taking place in the cell prior to substrate transport during conjugation.

Indexed as

Conjugation, GeneticCryoelectron MicroscopyDNA, BacterialDNA HelicasesDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsModels, MolecularDNA, BacterialDNA HelicasesDNA, Single-StrandedEscherichia coli ProteinsTraI protein, E colibacterial conjugationcryo-electron microscopyrelaxasestructural biologyTraItype IV secretion system

Identifiers

PMID28457609
PMCPMC5422253
OpenAlexW2607778061

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.