Evidence map›Paper›PMID 26744406›Full record

ArticleScience (New York, N.Y.)2016

The structure of the β-barrel assembly machinery complex.

Jeremy Bakelar, Susan K Buchanan, Nicholas Noinaj

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 163 papers.

0numbers the graph read from it
0cells of the map it votes in
163citing 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

163 citing papers in PubMed.

  1. Article
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  5. Article
  6. Review
  7. Review
  8. Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Bacterial cell envelope-targeting antibiotics.Nature reviews. Microbiology · 2026
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

103 more citing papers are in PubMed but not listed here.

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

3 authors.

Jeremy BakelarMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Susan K BuchananNational Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Nicholas NoinajMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA. nnoinaj@purdue.edu.

Funding

structural characterization of bacterial secretion channelsZIADK036139 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.3M
The role of BamA in the biogenesis of beta-barrel membrane proteinsK22AI113078 · NIAID · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2015 to 2016
$267k
Intramural NIH HHS ZIA DK036139NIAID NIH HHS 1K22AI113078-01NIAID NIH HHS K22 AI113078
6 · The paper itself

Abstract

β-Barrel outer membrane proteins (OMPs) are found in the outer membranes of Gram-negative bacteria and are essential for nutrient import, signaling, and adhesion. A 200-kilodalton five-component complex called the β-barrel assembly machinery (BAM) complex has been implicated in the biogenesis of OMPs. We report the structure of the BAM complex from Escherichia coli, revealing that binding of BamCDE modulates the conformation of BamA, the central component, which may serve to regulate the BAM complex. The periplasmic domain of BamA was in a closed state that prevents access to the barrel lumen, which indicates substrate OMPs may not be threaded through the barrel during biogenesis. Further, conformational shifts in the barrel domain lead to opening of the exit pore and rearrangement at the lateral gate.

Indexed as

Bacterial Outer Membrane ProteinsCrystallography, X-RayEscherichia coliEscherichia coli ProteinsMultiprotein ComplexesProtein Structure, SecondaryProtein Structure, TertiaryBacterial Outer Membrane ProteinsEscherichia coli ProteinsMultiprotein Complexes

Identifiers

PMID26744406
PMCPMC4883095

What OpenQuestion holds

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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.