Evidence map›Paper›PMID 33432152›Full record

ArticleNature microbiology2021

Structure and mechanism of the proton-driven motor that powers type 9 secretion and gliding motility.

Rory Hennell James, Justin C Deme, Andreas Kjӕr, Felicity Alcock, Augustinas Silale, Frédéric Lauber, Steven Johnson, Ben C Berks, Susan M Lea

Open access · greenAbstract read
In one paragraph

Article in Nature microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
12.5field-weighted citation impact, top 1% 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

54 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025
    Review
  17. Article
  18. Article
  19. TheJournal of oral microbiology · 2025
    Article
  20. A very versatile molecular machine.Journal of bacteriology · 2024
    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 1 institution in 1 country.

Rory Hennell James *Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Justin C Deme *Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-8811-9871
Andreas KjӕrDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-0096-5764
Felicity AlcockDepartment of Biochemistry, University of Oxford, Oxford, UK.
Augustinas SilaleDepartment of Biochemistry, University of Oxford, Oxford, UK.
Frédéric LauberDepartment of Biochemistry, University of Oxford, Oxford, UK.
Steven JohnsonSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-7877-3543
Ben C BerksDepartment of Biochemistry, University of Oxford, Oxford, UK. ben.berks@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0001-9685-4067
Susan M LeaSir William Dunn School of Pathology, University of Oxford, Oxford, UK. susan.lea@path.ox.ac.uk.ORCID http://orcid.org/0000-0001-9287-8053
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 100298Wellcome Trust 107929Wellcome Trust 109136Wellcome Trust 201536Wellcome Trust 209194/Z/17/Z
6 · The paper itself

Abstract

Three classes of ion-driven protein motors have been identified to date: ATP synthase, the bacterial flagellar motor and a proton-driven motor that powers gliding motility and the type 9 protein secretion system in Bacteroidetes bacteria. Here, we present cryo-electron microscopy structures of the gliding motility/type 9 protein secretion system motors GldLM from Flavobacterium johnsoniae and PorLM from Porphyromonas gingivalis. The motor is an asymmetric inner membrane protein complex in which the single transmembrane helices of two periplasm-spanning GldM/PorM proteins are positioned inside a ring of five GldL/PorL proteins. Mutagenesis and single-molecule tracking identify protonatable amino acid residues in the transmembrane domain of the complex that are important for motor function. Our data provide evidence for a mechanism in which proton flow results in rotation of the periplasm-spanning GldM/PorM dimer inside the intra-membrane GldL/PorL ring to drive processes at the bacterial outer membrane.

Indexed as

Bacterial ProteinsBacterial Secretion SystemsCryoelectron MicroscopyFlavobacteriumMovementPeriplasmPorphyromonas gingivalisProtein DomainsProtein MultimerizationProtonsSingle Molecule ImagingBacterial ProteinsBacterial Secretion SystemsProtons

Identifiers

PMID33432152
PMCPMC7116788
OpenAlexW3097536142

What OpenQuestion holds

Textmetadata
LicenceTDM
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.