Evidence map›Paper›PMID 33318620›Full record

ArticleCommunications biology2020

Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs.

Matthew G Iadanza, Bob Schiffrin, Paul White, Matthew A Watson, Jim E Horne, Anna J Higgins, Antonio N Calabrese, David J Brockwell, Roman Tuma, Antreas C Kalli and 2 more

Abstract read
In one paragraph

Article in Communications biology, 2020. 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
–field-weighted citation impact
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.

  1. Review
  2. Article
  3. Article
  4. Review
  5. A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Vaccines · 2024
    Review
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

12 authors.

Matthew G IadanzaAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Bob SchiffrinAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Paul WhiteAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Matthew A WatsonAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Jim E HorneAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Anna J HigginsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Antonio N CalabreseAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0003-2437-7761
David J BrockwellAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0002-0802-5937
Roman TumaAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0003-0047-0013
Antreas C KalliAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0001-7156-9403
Sheena E RadfordAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK. s.e.radford@leeds.ac.uk.ORCID 0000-0002-3079-8039
Neil A RansonAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK. n.a.ranson@leeds.ac.uk.ORCID 0000-0002-3640-5275

Funding

Biotechnology and Biological Sciences Research Council BB/M01151/1Biotechnology and Biological Sciences Research Council BB/N007603/1Biotechnology and Biological Sciences Research Council BB/N017307/1Biotechnology and Biological Sciences Research Council BB/P000037/1Biotechnology and Biological Sciences Research Council BB/T000635/1Medical Research Council MR/P018491/1Wellcome Trust 105220/Z/14/ZWellcome Trust 108466Wellcome Trust 108466/Z/15/ZWellcome Trust 208395Wellcome Trust 208395/Z/17/Z
6 · The paper itself

Abstract

The β-barrel assembly machinery (BAM) catalyses the folding and insertion of β-barrel outer membrane proteins (OMPs) into the outer membranes of Gram-negative bacteria by mechanisms that remain unclear. Here, we present an ensemble of cryoEM structures of the E. coli BamABCDE (BAM) complex in lipid nanodiscs, determined using multi-body refinement techniques. These structures, supported by single-molecule FRET measurements, describe a range of motions in the BAM complex, mostly localised within the periplasmic region of the major subunit BamA. The β-barrel domain of BamA is in a 'lateral open' conformation in all of the determined structures, suggesting that this is the most energetically favourable species in this bilayer. Strikingly, the BAM-containing lipid nanodisc is deformed, especially around BAM's lateral gate. This distortion is also captured in molecular dynamics simulations, and provides direct structural evidence for the lipid 'disruptase' activity of BAM, suggested to be an important part of its functional mechanism.

Indexed as

Lipid BilayersLipidsMolecular Dynamics SimulationNanostructuresProtein MultimerizationBacterial Outer Membrane ProteinsCatalysisMultiprotein ComplexesProtein ConformationProtein FoldingProteolipidsBacterial Outer Membrane ProteinsLipid BilayersLipidsMultiprotein ComplexesProteolipidsproteoliposomes

Identifiers

PMID33318620
PMCPMC7736308

What OpenQuestion holds

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Registered trials

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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.