Evidence map›Paper›PMID 26934982›Full record

ArticleBioscience reports2016

Structural model of FeoB, the iron transporter from Pseudomonas aeruginosa, predicts a cysteine lined, GTP-gated pore.

Saeed Seyedmohammad, Natalia Alveal Fuentealba, Robert A J Marriott, Tom A Goetze, J Michael Edwardson, Nelson P Barrera, Henrietta Venter

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Targeting Iron - Respiratory Reciprocity Promotes Bacterial Death.bioRxiv : the preprint server for biology · 2024
    Article
  9. Article
  10. Review
  11. 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. Review
  17. Metallomics : integrated biometal science · 2020
    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

7 authors at 2 institutions in 2 countries.

Saeed SeyedmohammadDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, U.K.
Natalia Alveal FuentealbaDepartment of Physiology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Santiago, Chile.
Robert A J MarriottSchool of Pharmacy and Medical Sciences, Sansom Institute for Health Research, University of South Australia, GPO Box 2471, Adelaide 5001, Australia.
Tom A GoetzeDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, U.K.
J Michael EdwardsonDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, U.K.
Nelson P BarreraDepartment of Physiology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Santiago, Chile rietie.venter@unisa.edu.au nbarrera@bio.puc.cl.
Henrietta VenterSchool of Pharmacy and Medical Sciences, Sansom Institute for Health Research, University of South Australia, GPO Box 2471, Adelaide 5001, Australia rietie.venter@unisa.edu.au nbarrera@bio.puc.cl.
Pontificia Universidad Católica de Chile · CLUniversity of South Australia · AU

Funding

Biotechnology and Biological Sciences Research Council F017464/1Wellcome Trust 089125/Z/09/Z
6 · The paper itself

Abstract

Iron is essential for the survival and virulence of pathogenic bacteria. The FeoB transporter allows the bacterial cell to acquire ferrous iron from its environment, making it an excellent drug target in intractable pathogens. The protein consists of an N-terminal GTP-binding domain and a C-terminal membrane domain. Despite the availability of X-ray crystal structures of the N-terminal domain, many aspects of the structure and function of FeoB remain unclear, such as the structure of the membrane domain, the oligomeric state of the protein, the molecular mechanism of iron transport, and how this is coupled to GTP hydrolysis at the N-terminal domain. In the present study, we describe the first homology model of FeoB. Due to the lack of sequence homology between FeoB and other transporters, the structures of four different proteins were used as templates to generate the homology model of full-length FeoB, which predicts a trimeric structure. We confirmed this trimeric structure by both blue-native-PAGE (BN-PAGE) and AFM. According to our model, the membrane domain of the trimeric protein forms a central pore lined by highly conserved cysteine residues. This pore aligns with a central pore in the N-terminal GTPase domain (G-domain) lined by aspartate residues. Biochemical analysis of FeoB from Pseudomonas aeruginosa further reveals a putative iron sensor domain that could connect GTP binding/hydrolysis to the opening of the pore. These results indicate that FeoB might not act as a transporter, but rather as a GTP-gated channel.

Indexed as

Models, MolecularBacterial ProteinsCation Transport ProteinsProtein DomainsProtein Structure, QuaternaryPseudomonas aeruginosaBacterial ProteinsCation Transport ProteinschannelFeoBGTPase (guanosine 5′-triphosphatase)homology modellingiron acquisitionmembrane proteinpathogen

Identifiers

PMID26934982
PMCPMC4847171
OpenAlexW2292216442

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Registered trials

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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.