Evidence map›Paper›PMID 12949103›Full record

ArticleJournal of bacteriology2003

In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12.

Michael Braun, Franziska Endriss, Helmut Killmann, Volkmar Braun

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Outer Membrane Biogenesis.Annual review of microbiology · 2017
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  11. Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  12. FhuA (TonA), the career of a protein.Journal of bacteriology · 2009
    Review
  13. Structure and function of Pseudomonas aeruginosa protein PA1324 (21-170).Protein science : a publication of the Protein Society · 2009
    Article
  14. Article
  15. Article
  16. Purification, crystallization and preliminary X-ray analysis of the outer membrane complex HasA-HasR from Serratia marcescens.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006
    Article
  17. Article
  18. 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

4 authors at 1 institution in 1 country.

Michael BraunMikrobiologie/Membranphysiologie, Universität Tübingen, D-72076 Tübingen, Germany.
Franziska Endriss
Helmut Killmann
Volkmar Braun
University of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The FhuA protein in the outer membrane of Escherichia coli actively transports ferrichrome and the antibiotics albomycin and rifamycin CGP 4832 and serves as a receptor for the phages T1, T5, and phi80 and for colicin M and microcin J25. The crystal structure reveals a beta-barrel with a globular domain, the cork, which closes the channel formed by the barrel. Genetic deletion of the cork resulted in a beta-barrel that displays no FhuA activity. A functional FhuA was obtained by cosynthesis of separately encoded cork and the beta-barrel domain, each endowed with a signal sequence, which showed that complementation occurs after secretion of the fragments across the cytoplasmic membrane. Inactive complete mutant FhuA and an FhuA fragment containing 357 N-proximal amino acid residues complemented the separately synthesized wild-type beta-barrel to form an active FhuA. Previous claims that the beta-barrel is functional as transporter and receptor resulted from complementation by inactive complete FhuA and the 357-residue fragment. No complementation was observed between the wild-type cork and complete but inactive FhuA carrying cork mutations that excluded the exchange of cork domains. The data indicate that active FhuA is reconstituted extracytoplasmically by insertion of separately synthesized cork or cork from complete FhuA into the beta-barrel, and they suggest that in wild-type FhuA the beta-barrel is formed prior to the insertion of the cork.

Indexed as

Bacterial Outer Membrane ProteinsBase SequenceBiological TransportCytoplasmEscherichia coliEscherichia coli ProteinsFerrichromeGenetic Complementation TestMolecular Sequence DataMutationPeriplasmPlasmidsProtein ConformationProtein Structure, TertiaryReceptors, VirusBacterial Outer Membrane ProteinsEscherichia coli ProteinsFerrichromeFhuA protein, E coliReceptors, Virus

Identifiers

PMID12949103
PMCPMC193757
OpenAlexW2127623706

What OpenQuestion holds

Textmetadata
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.