Evidence map›Paper›PMID 27612581›Full record

ArticleJournal of structural biology2016

Structures of type IV pilins from Thermus thermophilus demonstrate similarities with type II secretion system pseudopilins.

Vijaykumar Karuppiah, Angela Thistlethwaite, Jeremy P Derrick

Open access · hybridAbstract read
In one paragraph

Article in Journal of structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. β-strand addition within tip initiation complexes licenses assembly of diverse type IV filaments.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Expression of soluble Type IV Minor Pilins and isolation of abioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Stimulation of themBio · 2025
    Article
  7. Review
  8. Article
  9. Structure and function of minor pilins of type IV pili.Medical microbiology and immunology · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. DNA Uptake by Type IV Filaments.Frontiers in molecular biosciences · 2019
    Review
  15. 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

3 authors at 1 institution in 1 country.

Vijaykumar KaruppiahMichael Smith Building, Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester, UK.
Angela ThistlethwaiteMichael Smith Building, Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester, UK.
Jeremy P DerrickMichael Smith Building, Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester, UK. Electronic address: Jeremy.Derrick@manchester.ac.uk.
University of Manchester · GB

Funding

Wellcome Trust 093388/Z/10/Z
6 · The paper itself

Abstract

Type IV pilins are proteins which form polymers that extend from the surface of the bacterial cell; they are involved in mediating a wide variety of functions, including adhesion, motility and natural competence. Here we describe the determination of the crystal structures of three type IVa pilins proteins from the thermophile Thermus thermophilus. They form part of a cluster of pilus-like proteins within the genome; our results show that one, Tt1222, is very closely related to the main structural type IV pilin, PilA4. The other two, Tt1218 and Tt1219, also adopt canonical pilin-like folds but, interestingly, are most closely related to the structures of the type II secretion system pseudopilins, EpsI/GspI and XcpW/GspJ. GspI and GspJ have been shown to form a complex with another pseudopilin, GspK, and this heterotrimeric complex is known to play a key role in initiating assembly of a pseudopilus which is thought to drive the secretion process. The structural similarity of Tt1218 and Tt1219 to GspI and GspJ suggests that they might work in a similar way, to deliver functions associated with type IV pili in T. thermophilus, such as natural competence.

Indexed as

Crystallography, X-RayEscherichia coliEscherichia coli ProteinsFimbriae ProteinsModels, MolecularPseudomonas aeruginosaThermus thermophilusType II Secretion SystemsEscherichia coli ProteinsFimbriae ProteinsGspI protein, E coliGspJ protein, E coliType II Secretion SystemsNatural competencePilusThermophileType II secretion systemX-ray crystallography

Identifiers

PMID27612581
PMCPMC5131608
OpenAlexW2515307509

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.