Evidence map›Paper›PMID 41299015›Full record

ArticleCommunications biology2025

Structure of the conjugation surface exclusion protein TraT.

Nicolas Chen, Alfredas Bukys, Camilla A K Lundgren, Justin C Deme, Hafez El Sayyed, Achillefs N Kapanidis, Susan M Lea, Ben C Berks

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PubMed Full text at PMC Publisher
In one paragraph

Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Nicolas ChenDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0009-0007-2421-8468
Alfredas Bukys *Department of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0009-0007-9250-9005
Camilla A K Lundgren *Department of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-8854-6937
Justin C DemeCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, Frederick, MD, USA.ORCID http://orcid.org/0000-0001-8811-9871
Hafez El SayyedBiological Physics Research Group, Department of Physics, University of Oxford, Oxford, UK.
Achillefs N KapanidisBiological Physics Research Group, Department of Physics, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-6699-136X
Susan M LeaCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, Frederick, MD, USA. susan.lea@stjude.org.ORCID http://orcid.org/0000-0001-9287-8053
Ben C BerksDepartment of Biochemistry, University of Oxford, Oxford, UK. ben.berks@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0001-9685-4067

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 833713Merton College, University of Oxford (Merton College Oxford) ScholarshipRCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/S007474/1University of Oxford (Oxford University) Clarendon ScholarshipWellcome TrustWellcome Trust (Wellcome) 226662/Z/22/Z
6 · The paper itself

Abstract

Conjugal transfer of plasmids between bacteria is a major route for the spread of antimicrobial resistance. Many conjugative plasmids encode exclusion systems that inhibit redundant conjugation. In incompatibility group F (IncF) plasmids surface exclusion is mediated by the outer membrane protein TraT. Here we report the cryoEM structure of the TraT exclusion protein complex from the canonical F plasmid of Escherichia coli. TraT is a hollow homodecamer shaped like a chef's hat. In contrast to most outer membrane proteins, TraT spans the outer membrane using transmembrane α-helices. We develop a microscopy-based conjugation assay to probe the effects of directed mutagenesis on TraT. Our analysis provides no support for the idea that TraT has specific interactions with partner proteins. Instead, we infer that TraT is most likely to function by physical interference with conjugation. This work provides structural insight into a natural inhibitor of microbial gene transfer.

Indexed as

Bacterial Outer Membrane ProteinsConjugation, GeneticEscherichia coliEscherichia coli ProteinsCryoelectron MicroscopyModels, MolecularProtein ConformationBacterial Outer Membrane ProteinsEscherichia coli Proteins

Identifiers

PMID41299015
PMCPMC12658005

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Registered trials

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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.