Evidence map›Paper›PMID 37019934›Full record

ArticleNature communications2023

Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome.

Hong Thuy Vy Nguyen, Xiaorui Chen, Claudia Parada, An-Chi Luo, Orion Shih, U-Ser Jeng, Chia-Ying Huang, Yu-Ling Shih, Che Ma

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.9field-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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. In Silico Druggability Assessment ofAntibiotics (Basel, Switzerland) · 2026
    Article
  6. Article
  7. FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
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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 6 institutions in 2 countries.

Hong Thuy Vy Nguyen *Genomics Research Center, Academia Sinica, Taipei, 115, Taiwan.ORCID 0000-0001-7577-3452
Xiaorui Chen *Genomics Research Center, Academia Sinica, Taipei, 115, Taiwan.ORCID 0000-0002-4492-0883
Claudia ParadaInstitute of Biological Chemistry, Academia Sinica, Taipei, 115, Taiwan.ORCID 0000-0003-3594-3730
An-Chi LuoInstitute of Biochemical Sciences, National Taiwan University, Taipei, 10617, Taiwan.
Orion ShihNational Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan.
U-Ser JengNational Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan.
Chia-Ying HuangPaul Scherrer Institute, Forschungsstrasse 111, Villigen-PSI, 5232, Switzerland.ORCID 0000-0002-7676-0239
Yu-Ling ShihInstitute of Biochemical Sciences, National Taiwan University, Taipei, 10617, Taiwan. ylshih10@gate.sinica.edu.tw.ORCID 0000-0002-8232-2569
Che MaGenomics Research Center, Academia Sinica, Taipei, 115, Taiwan. cma@gate.sinica.edu.tw.ORCID 0000-0002-4741-2307
National Taiwan University · TWGenomics Research Center, Academia Sinica · TWInstitute of Biological Chemistry, Academia Sinica · TWNational Synchrotron Radiation Research Center · TWNational Tsing Hua University · TWPaul Scherrer Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synthesis of the cell-wall peptidoglycan during bacterial cell division is mediated by a multiprotein machine, called the divisome. The essential membrane protein complex of FtsB, FtsL and FtsQ (FtsBLQ) is at the heart of the divisome assembly cascade in Escherichia coli. This complex regulates the transglycosylation and transpeptidation activities of the FtsW-FtsI complex and PBP1b via coordination with FtsN, the trigger for the onset of constriction. Yet the underlying mechanism of FtsBLQ-mediated regulation is largely unknown. Here, we report the full-length structure of the heterotrimeric FtsBLQ complex, which reveals a V-shaped architecture in a tilted orientation. Such a conformation could be strengthened by the transmembrane and the coiled-coil domains of the FtsBL heterodimer, as well as an extended β-sheet of the C-terminal interaction site involving all three proteins. This trimeric structure may also facilitate interactions with other divisome proteins in an allosteric manner. These results lead us to propose a structure-based model that delineates the mechanism of the regulation of peptidoglycan synthases by the FtsBLQ complex.

Indexed as

Escherichia coli ProteinsBacterial ProteinsCell Cycle ProteinsCell DivisionEscherichia coliMembrane ProteinsPeptidoglycanBacterial ProteinsCell Cycle ProteinsEscherichia coli ProteinsFtsB protein, E coliftsL protein, E coliFtsQ protein, E coliMembrane ProteinsPeptidoglycan

Identifiers

PMID37019934
PMCPMC10076392
OpenAlexW4362604766

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.