Evidence map›Paper›PMID 23584587›Full record

ArticleNature2013

Structure of a bacterial energy-coupling factor transporter.

Tingliang Wang, Guobin Fu, Xiaojing Pan, Jianping Wu, Xinqi Gong, Jiawei Wang, Yigong Shi

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.5field-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

37 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. The Evolution of ABC Importers.Journal of molecular biology · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Insights into the bilayer-mediated toppling mechanism of a folate-specific ECF transporter by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Review
  13. Heme Uptake inApplied and environmental microbiology · 2020
    Article
  14. Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020
    Review
  15. Article
  16. Article
  17. Review
  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

7 authors at 2 institutions in 1 country.

Tingliang WangMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
Guobin Fu
Xiaojing Pan
Jianping Wu
Xinqi Gong
Jiawei Wang
Yigong Shi
Tsinghua University · CNCenter for Life Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The energy-coupling factor (ECF) transporters constitute a novel family of conserved membrane transporters in prokaryotes that have a similar domain organization to the ATP-binding cassette transporters. Each ECF transporter comprises a pair of cytosolic ATPases (the A and A' components, or EcfA and EcfA'), a membrane-embedded substrate-binding protein (the S component, or EcfS) and a transmembrane energy-coupling component (the T component, or EcfT) that links the EcfA-EcfA' subcomplex to EcfS. The structure and transport mechanism of the quaternary ECF transporter remain largely unknown. Here we report the crystal structure of a nucleotide-free ECF transporter from Lactobacillus brevis at a resolution of 3.5 Å. The T component has a horseshoe-shaped open architecture, with five α-helices as transmembrane segments and two cytoplasmic α-helices as coupling modules connecting to the A and A' components. Strikingly, the S component, thought to be specific for hydroxymethyl pyrimidine, lies horizontally along the lipid membrane and is bound exclusively by the five transmembrane segments and the two cytoplasmic helices of the T component. These structural features suggest a plausible working model for the transport cycle of the ECF transporters.

Indexed as

Anti-Bacterial AgentsATP-Binding Cassette TransportersBacterial ProteinsCrystallography, X-RayCytoplasmLevilactobacillus brevisModels, BiologicalModels, MolecularProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsPyrimidinesStructure-Activity RelationshipSubstrate SpecificityAnti-Bacterial AgentsATP-Binding Cassette TransportersBacterial ProteinsProtein SubunitsPyrimidines

Identifiers

PMID23584587
OpenAlexW2077555752

What OpenQuestion holds

Textmetadata
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.