Evidence map›Paper›PMID 23104801›Full record

ArticleJournal of bacteriology2013

Solution structure of Escherichia coli FeoA and its potential role in bacterial ferrous iron transport.

Cheryl K Y Lau, Hiroaki Ishida, Zhihong Liu, Hans J Vogel

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Tevenvirinae phages encode a family of LSm-like fold proteins.Computational and structural biotechnology journal · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. MAT Gain of Activity Mutation inACS infectious diseases · 2023
    Article
  12. Article
  13. Article
  14. The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  15. Recent Advances in the Siderophore Biology ofFrontiers in microbiology · 2022
    Review
  16. Investigation ofFoods (Basel, Switzerland) · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Proceedings of the National Academy of Sciences of the United States of America · 2019
    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.

Cheryl K Y LauBiochemistry Research Group, Department of Biological Sciences, University of Calgary, Alberta, Canada.
Hiroaki Ishida
Zhihong Liu
Hans J Vogel
University of Calgary · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Iron is an indispensable nutrient for most organisms. Ferric iron (Fe(3+)) predominates under aerobic conditions, while during oxygen limitation ferrous (Fe(2+)) iron is usually present. The Feo system is a bacterial ferrous iron transport system first discovered in Escherichia coli K-12. It consists of three genes, feoA, feoB, and feoC (yhgG). FeoB is thought to be the main transmembrane transporter while FeoC is considered to be a transcriptional regulator. Using multidimensional nuclear magnetic resonance (NMR) spectroscopy, we have determined the solution structure of E. coli FeoA. The structure of FeoA reveals a Src-homology 3 (SH3)-like fold. The structure is composed of a β-barrel with two α-helices where one helix is positioned over the barrel. In comparison to the standard eukaryotic SH3 fold, FeoA has two additional α-helices. FeoA was further characterized by heteronuclear NMR dynamics measurements, which suggest that it is a monomeric, stable globular protein. Model-free analysis of the NMR relaxation results indicates that a slow conformational dynamic process is occurring in β-strand 4 that may be important for function. (31)P NMR-based GTPase activity measurements with the N-terminal domain of FeoB (NFeoB) indicate a higher GTP hydrolysis rate in the presence of potassium than with sodium. Further enzymatic assays with NFeoB suggest that FeoA may not act as a GTPase-activating protein as previously proposed. These findings, together with bioinformatics and structural analyses, suggest that FeoA may have a different role, possibly interacting with the cytoplasmic domain of the highly conserved core portion of the FeoB transmembrane region.

Indexed as

Biological Transport, ActiveCation Transport ProteinsCloning, MolecularEscherichiaEscherichia coli ProteinsGene Expression Regulation, BacterialMembrane Transport ProteinsModels, MolecularMutagenesis, Site-DirectedMutationNuclear Magnetic Resonance, BiomolecularOxidoreductasesProtein ConformationCation Transport ProteinsEscherichia coli ProteinsFeoB protein, E colifeo protein, E coliiron oxidase, Thiobacillus ferrooxidansMembrane Transport ProteinsOxidoreductases

Identifiers

PMID23104801
PMCPMC3536175
OpenAlexW2097229477

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.