Evidence map›Paper›PMID 27161979›Full record

ArticleStructure (London, England : 1993)2016

A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.

Jamie-Lee Berry, Yingqi Xu, Philip N Ward, Susan M Lea, Stephen J Matthews, Vladimir Pelicic

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Characterization of a glycan-binding complex of minor pilins completes the analysis ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Multisite transformation inFrontiers in microbiology · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. The minor pilin PilV provides a conserved adhesion site throughout the antigenically variable meningococcal type IV pilus.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. 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

6 authors.

Jamie-Lee BerryMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Yingqi XuCentre for Structural Biology, Imperial College London, London SW7 2AZ, UK.
Philip N WardSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Susan M LeaSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Stephen J MatthewsCentre for Structural Biology, Imperial College London, London SW7 2AZ, UK. Electronic address: s.j.matthews@imperial.ac.uk.
Vladimir PelicicMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK. Electronic address: v.pelicic@imperial.ac.uk.

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MR/J006874/1Wellcome Trust
6 · The paper itself

Abstract

DNA transformation is a widespread process allowing bacteria to capture free DNA by using filamentous nano-machines composed of type IV pilins. These proteins can act as DNA receptors as demonstrated by the finding that Neisseria meningitidis ComP minor pilin has intrinsic DNA-binding ability. ComP binds DNA better when it contains the DNA-uptake sequence (DUS) motif abundant in this species genome, playing a role in its trademark ability to selectively take up its own DNA. Here, we report high-resolution structures for meningococcal ComP and Neisseria subflava ComPsub, which recognize different DUS motifs. We show that they are structurally identical type IV pilins that pack readily into filament models and display a unique DD region delimited by two disulfide bonds. Functional analysis of ComPsub defines a new mode of DNA binding involving the DD region, adapted for exported DNA receptors.

Indexed as

Amino Acid MotifsBinding SitesCrystallography, X-RayDNA, BacterialFimbriae, BacterialFimbriae ProteinsModels, MolecularNeisseriaProtein BindingProtein ConformationProtein FoldingDNA, BacterialFimbriae Proteins

Identifiers

PMID27161979
PMCPMC4906244

What OpenQuestion holds

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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.