Evidence map›Paper›PMID 26749448›Full record

ArticleStructure (London, England : 1993)2016

The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core.

Hans Thor Bergal, Alex Hunt Hopkins, Sandra Ines Metzner, Marcelo Carlos Sousa

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. 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
3.7field-weighted citation impact, top 6% 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, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020
    Review
  10. Article
  11. Review
  12. Article
  13. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  14. Insertion of proteins and lipopolysaccharide into the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  15. Review
  16. The β-barrel assembly machinery in motion.Nature reviews. Microbiology · 2017
    Review
  17. Article
  18. From Chaperones to the Membrane with a BAM!Trends in biochemical sciences · 2016
    Review
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Hans Thor BergalDepartment of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.
Alex Hunt HopkinsDepartment of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.
Sandra Ines MetznerDepartment of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.
Marcelo Carlos SousaDepartment of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA. Electronic address: marcelo.sousa@colorado.edu.
University of Colorado Boulder · US

Funding

Transport and Insertion of Outer Membrane ProteinsR01AI080709 · NIAID · UNIVERSITY OF COLORADO · PI SOUSA, MARCELO C. · 2009 to 2016
$2.6M
NIAID NIH HHS R01 AI080709
6 · The paper itself

Abstract

The β-barrel assembly machine (BAM) mediates folding and insertion of integral β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria. Of the five BAM subunits, only BamA and BamD are essential for cell viability. Here we present the crystal structure of a fusion between BamA POTRA4-5 and BamD from Rhodothermus marinus. The POTRA5 domain binds BamD between its tetratricopeptide repeats 3 and 4. The interface structural elements are conserved in the Escherichia coli proteins, which allowed structure validation by mutagenesis and disulfide crosslinking in E. coli. Furthermore, the interface is consistent with previously reported mutations that impair BamA-BamD binding. The structure serves as a linchpin to generate a BAM model where POTRA domains and BamD form an elongated periplasmic ring adjacent to the membrane with a central cavity approximately 30 × 60 Å wide. We propose that nascent OMPs bind this periplasmic ring prior to insertion and folding by BAM.

Indexed as

Bacterial Outer Membrane ProteinsBinding SitesModels, MolecularMutationProtein BindingProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsRhodothermusBacterial Outer Membrane ProteinsRecombinant Fusion Proteins

Identifiers

PMID26749448
PMCPMC4740259
OpenAlexW2197818756

What OpenQuestion holds

Textmetadata
LicenceTDM
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.