Evidence map›Paper›PMID 30420757›Full record

ArticleNature communications2018

Structural insights into the function of type VI secretion system TssA subunits.

Samuel R Dix, Hayley J Owen, Ruyue Sun, Asma Ahmad, Sravanthi Shastri, Helena L Spiewak, Daniel J Mosby, Matthew J Harris, Sarah L Batters, Thomas A Brooker and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. The multifunctional type VI secretion system ofApplied and environmental microbiology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. ThebioRxiv : the preprint server for biology · 2023
    Article
  11. The type-VI secretion system of the beneficial symbiontMicrobiology (Reading, England) · 2023
    Review
  12. Uncovering the Secretion Systems ofAntibiotics (Basel, Switzerland) · 2023
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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
  19. Article
  20. 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

16 authors at 3 institutions in 1 country.

Samuel R DixDepartment of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK.ORCID http://orcid.org/0000-0002-6907-1435
Hayley J OwenDepartment of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK.
Ruyue SunDepartment of Infection, Immunity and Cardiovascular Disease, University of Sheffield Medical School, Beech Hill Road, Sheffield, S10 2RX, UK.ORCID http://orcid.org/0000-0003-3192-7290
Asma AhmadDepartment of Infection, Immunity and Cardiovascular Disease, University of Sheffield Medical School, Beech Hill Road, Sheffield, S10 2RX, UK.
Sravanthi ShastriDepartment of Infection, Immunity and Cardiovascular Disease, University of Sheffield Medical School, Beech Hill Road, Sheffield, S10 2RX, UK.
Helena L SpiewakDepartment of Infection, Immunity and Cardiovascular Disease, University of Sheffield Medical School, Beech Hill Road, Sheffield, S10 2RX, UK.ORCID http://orcid.org/0000-0003-1039-5520
Daniel J MosbyDepartment of Infection, Immunity and Cardiovascular Disease, University of Sheffield Medical School, Beech Hill Road, Sheffield, S10 2RX, UK.
Matthew J HarrisDepartment of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK.
Sarah L BattersDepartment of Infection, Immunity and Cardiovascular Disease, University of Sheffield Medical School, Beech Hill Road, Sheffield, S10 2RX, UK.
Thomas A BrookerDepartment of Infection, Immunity and Cardiovascular Disease, University of Sheffield Medical School, Beech Hill Road, Sheffield, S10 2RX, UK.
Svetomir B TzokovDepartment of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK.ORCID http://orcid.org/0000-0001-7256-5279
Svetlana E SedelnikovaDepartment of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK.
Patrick J BakerDepartment of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK.ORCID http://orcid.org/0000-0003-1995-5643
Per A BulloughDepartment of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK.
David W RiceDepartment of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK. d.rice@sheffield.ac.uk.
Mark S ThomasDepartment of Infection, Immunity and Cardiovascular Disease, University of Sheffield Medical School, Beech Hill Road, Sheffield, S10 2RX, UK. m.s.thomas@sheffield.ac.uk.ORCID http://orcid.org/0000-0003-0701-2584
University of Sheffield · GBKing's College London · GBNewcastle upon Tyne Hospitals NHS Foundation Trust · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The type VI secretion system (T6SS) is a multi-protein complex that injects bacterial effector proteins into target cells. It is composed of a cell membrane complex anchored to a contractile bacteriophage tail-like apparatus consisting of a sharpened tube that is ejected by the contraction of a sheath against a baseplate. We present structural and biochemical studies on TssA subunits from two different T6SSs that reveal radically different quaternary structures in comparison to the dodecameric E. coli TssA that arise from differences in their C-terminal sequences. Despite this, the different TssAs retain equivalent interactions with other components of the complex and position their highly conserved N-terminal ImpA_N domain at the same radius from the centre of the sheath as a result of their distinct domain architectures, which includes additional spacer domains and highly mobile interdomain linkers. Together, these variations allow these distinct TssAs to perform a similar function in the complex.

Indexed as

Bacterial Secretion SystemsAmino Acid SequenceBacterial ProteinsComputational BiologyPhylogenyProtein DomainsProtein SubunitsProteolysisStructure-Activity RelationshipBacterial ProteinsBacterial Secretion SystemsProtein Subunits

Identifiers

PMID30420757
PMCPMC6232143
OpenAlexW2899736150

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.