Evidence map›Paper›PMID 37393310›Full record

ArticleNature communications2023

Architecture of a complete Bce-type antimicrobial peptide resistance module.

Natasha L George, Benjamin J Orlando

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. LiaS-dependent activation of the MadR regulon enables cross-talk betweenbioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Article
  10. The extracellular domain ofFrontiers in microbiology · 2025
    Article
  11. ScymicrosinFrontiers in microbiology · 2025
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. TheJournal of bacteriology · 2024
    Article
  18. mBio · 2024
    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

2 authors at 1 institution in 1 country.

Natasha L GeorgeDept. of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA.
Benjamin J OrlandoDept. of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA. orlandob@msu.edu.ORCID 0000-0001-7079-8140
Michigan State University · US

Funding

Midwest Consortium for High Resolution Cryoelectron MicroscopyU24GM116789 · NIGMS · PURDUE UNIVERSITY · PI BULLITT, ESTHER, DAI, WEI · 2017 to 2021
$3.5M
Structural Basis of Antimicrobial Peptide Sensing and ResistanceR35GM146721 · NIGMS · MICHIGAN STATE UNIVERSITY · PI Benjamin Joseph Orlando · 2022 to 2026
$1.9M
NIGMS NIH HHS R35 GM146721NIGMS NIH HHS U24 GM116789
6 · The paper itself

Abstract

Gram-positive bacteria synthesize and secrete antimicrobial peptides that target the essential process of peptidoglycan synthesis. These antimicrobial peptides not only regulate the dynamics of microbial communities but are also of clinical importance as exemplified by peptides such as bacitracin, vancomycin, and daptomycin. Many gram-positive species have evolved specialized antimicrobial peptide sensing and resistance machinery known as Bce modules. These modules are membrane protein complexes formed by an unusual Bce-type ABC transporter interacting with a two-component system sensor histidine kinase. In this work, we provide the first structural insight into how the membrane protein components of these modules assemble into a functional complex. A cryo-EM structure of an entire Bce module revealed an unexpected mechanism of complex assembly, and extensive structural flexibility in the sensor histidine kinase. Structures of the complex in the presence of a non-hydrolysable ATP analog reveal how nucleotide binding primes the complex for subsequent activation. Accompanying biochemical data demonstrate how the individual membrane protein components of the complex exert functional control over one another to create a tightly regulated enzymatic system.

Indexed as

Antimicrobial PeptidesPeptidesATP-Binding Cassette TransportersHistidine KinaseMembrane ProteinsAntimicrobial PeptidesATP-Binding Cassette TransportersHistidine KinaseMembrane ProteinsPeptides

Identifiers

PMID37393310
PMCPMC10314905
OpenAlexW4382794618

What OpenQuestion holds

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LicenceCC BY
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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.