Evidence map›Paper›PMID 29307484›Full record

ArticleStructure (London, England : 1993)2018

Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa.

Osman Salih, Shaoda He, Sara Planamente, Lasse Stach, James T MacDonald, Eleni Manoli, Sjors H W Scheres, Alain Filloux, Paul S Freemont

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Fine structure and assembly pattern of a minimal myophage Pam3.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A novel stabilization mechanism for the type VI secretion system sheath.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. TheFrontiers in microbiology · 2019
    Article
  19. 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

9 authors at 2 institutions in 1 country.

Osman SalihSection of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK.
Shaoda HeMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Sara PlanamenteMRC Centre for Molecular Bacteriology and Infection (CMBI), Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
Lasse StachSection of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK.
James T MacDonaldSection of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK.
Eleni ManoliMRC Centre for Molecular Bacteriology and Infection (CMBI), Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
Sjors H W ScheresMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Alain FillouxMRC Centre for Molecular Bacteriology and Infection (CMBI), Department of Life Sciences, Imperial College London, London SW7 2AZ, UK. Electronic address: a.filloux@imperial.ac.uk.
Paul S FreemontSection of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK. Electronic address: p.freemont@imperial.ac.uk.
Imperial College London · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_A025_1013Medical Research Council MR/K001930/1Medical Research Council MR/P028225/1
6 · The paper itself

Abstract

Pseudomonas aeruginosa has three type VI secretion systems (T6SSs), H1-, H2-, and H3-T6SS, each belonging to a distinct group. The two T6SS components, TssB/VipA and TssC/VipB, assemble to form tubules that conserve structural/functional homology with tail sheaths of contractile bacteriophages and pyocins. Here, we used cryoelectron microscopy to solve the structure of the H1-T6SS P. aeruginosa TssB1C1 sheath at 3.3 Å resolution. Our structure allowed us to resolve some features of the T6SS sheath that were not resolved in the Vibrio cholerae VipAB and Francisella tularensis IglAB structures. Comparison with sheath structures from other contractile machines, including T4 phage and R-type pyocins, provides a better understanding of how these systems have conserved similar functions/mechanisms despite evolution. We used the P. aeruginosa R2 pyocin as a structural template to build an atomic model of the TssB1C1 sheath in its extended conformation, allowing us to propose a coiled-spring-like mechanism for T6SS sheath contraction.

Indexed as

Models, MolecularBacterial ProteinsBacteriophage T4Cryoelectron MicroscopyPseudomonas aeruginosaType VI Secretion SystemsBacterial ProteinsType VI Secretion Systemsbacteriophagecryo-EMhelical structuremolecular evolutionT6SS

Identifiers

PMID29307484
PMCPMC5807055
OpenAlexW2782100329

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.