Evidence map›Paper›PMID 34294704›Full record

ArticleNature communications2021

Structure of the molecular bushing of the bacterial flagellar motor.

Tomoko Yamaguchi, Fumiaki Makino, Tomoko Miyata, Tohru Minamino, Takayuki Kato, Keiichi Namba

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
7.1field-weighted citation impact, top 3% 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

38 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Characterization of the role of putativeJournal of bacteriology · 2026
    Article
  6. The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026
    Review
  7. Pathogens (Basel, Switzerland) · 2025
    Article
  8. Article
  9. Article
  10. FlgY, PflA, and PflB form a spoke-ring network in the high-torque flagellar motor ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Discovery of Two Novel Immunoepitopes and Development of a Peptide-based Sarcoidosis Immunoassay.American journal of respiratory and critical care medicine · 2024
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  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 at 5 institutions in 1 country.

Tomoko Yamaguchi *Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.ORCID 0000-0001-9482-8738
Fumiaki Makino *Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.ORCID 0000-0001-9512-7087
Tomoko MiyataGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.ORCID 0000-0002-5543-7459
Tohru MinaminoGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.ORCID 0000-0002-8175-1951
Takayuki KatoGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan. tkato@protein.osaka-u.ac.jp.ORCID 0000-0002-8879-6685
Keiichi NambaGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan. keiichi@fbs.osaka-u.ac.jp.ORCID 0000-0003-2911-5875
The University of Osaka · JPJEOL (Japan) · JPOsaka Gakuin University · JPRIKEN Center for Biosystems Dynamics Research · JPSPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The basal body of the bacterial flagellum is a rotary motor that consists of several rings (C, MS and LP) and a rod. The LP ring acts as a bushing supporting the distal rod for its rapid and stable rotation without much friction. Here, we use electron cryomicroscopy to describe the LP ring structure around the rod, at 3.5 Å resolution, from Salmonella Typhimurium. The structure shows 26-fold rotational symmetry and intricate intersubunit interactions of each subunit with up to six partners, which explains the structural stability. The inner surface is charged both positively and negatively. Positive charges on the P ring (the part of the LP ring that is embedded within the peptidoglycan layer) presumably play important roles in its initial assembly around the rod with a negatively charged surface.

Indexed as

Bacterial ProteinsBasal BodiesCryoelectron MicroscopyFlagellaModels, MolecularMolecular Motor ProteinsMovementProtein Interaction Domains and MotifsProtein Structure, QuaternaryProtein SubunitsSalmonella typhimuriumStatic ElectricityBacterial ProteinsMolecular Motor ProteinsProtein Subunits

Identifiers

PMID34294704
PMCPMC8298488
OpenAlexW3186463678

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.