Evidence map›Paper›PMID 23024345›Full record

ArticleJournal of bacteriology2012

Crystal structure of the Klebsiella pneumoniae NFeoB/FeoC complex and roles of FeoC in regulation of Fe2+ transport by the bacterial Feo system.

Kuo-Wei Hung, Jia-Yin Tsai, Tzu-Hsuan Juan, Yen-Lan Hsu, Chwan-Deng Hsiao, Tai-Huang Huang

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2012. 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
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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. The structure of the full catalytic cycle ofbioRxiv : the preprint server for biology · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. 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
  8. Article
  9. Metallomics : integrated biometal science · 2020
    Article
  10. Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020
    Review
  11. Article
  12. Toward a mechanistic understanding of Feo-mediated ferrous iron uptake.Metallomics : integrated biometal science · 2018
    Review
  13. Article
  14. TheFrontiers in cellular and infection microbiology · 2017
    Article
  15. Article
  16. 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

6 authors at 3 institutions in 1 country.

Kuo-Wei HungInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.
Jia-Yin Tsai
Tzu-Hsuan Juan
Yen-Lan Hsu
Chwan-Deng Hsiao
Tai-Huang Huang
Institute of Biomedical Sciences, Academia Sinica · TWInstitute of Molecular Biology, Academia Sinica · TWNational Taiwan Normal University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Feo is a transport system commonly used by bacteria to acquire environmental Fe(2+). It consists of three proteins: FeoA, FeoB, and FeoC. FeoB is a large protein with a cytosolic N-terminal domain (NFeoB) that contains a regulatory G protein domain and a helical S domain. The C-terminal region of FeoB is a transmembrane domain that likely acts as the Fe(2+) permease. NFeoB has been shown to form a trimer pore that may function as an Fe(2+) gate. FeoC is a small winged-helix protein that possesses four conserved cysteine residues with a consensus sequence that likely provides binding sites for the [Fe-S] cluster. Therefore, FeoC is presumed to be an [Fe-S] cluster-dependent regulator that directly controls transcription of the feo operon. Despite the apparent significance of the Feo system, however, the function of FeoC has not been experimentally demonstrated. Here, we show that Klebsiella pneumoniae FeoC (KpFeoC) forms a tight complex with the intracellular N-terminal domain of FeoB (KpNFeoB). The crystal structure of the complex reveals that KpFeoC binds to KpNFeoB between the switch II region of the G protein domain and the effector S domain and that the long KpFeoC W1 loop lies above the KpNFeoB nucleotide-binding site. These interactions suggest that KpFeoC modulates the guanine nucleotide-mediated signal transduction process. Moreover, we showed that binding of KpFeoC disrupts pore formation by interfering with KpNFeoB trimerization. These results provide strong evidence suggesting that KpFeoC plays a crucial role in regulating Fe(2+) transport in Klebsiella pneumonia in addition to the presumed gene regulator role.

Indexed as

Bacterial ProteinsCrystallography, X-RayIronKlebsiella pneumoniaeMembrane Transport ProteinsModels, MolecularProtein BindingProtein MultimerizationProtein Structure, QuaternaryBacterial ProteinsIronMembrane Transport Proteins

Identifiers

PMID23024345
PMCPMC3497523
OpenAlexW2127957332

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.