Evidence map›Paper›PMID 27529188›Full record

ArticleeLife2016

Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments.

Didi He, Sam Hughes, Sally Vanden-Hehir, Atanas Georgiev, Kirsten Altenbach, Emma Tarrant, C Logan Mackay, Kevin J Waldron, David J Clarke, Jon Marles-Wright

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
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

47 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Characterization of Iron Oxide Nanoparticles Inside theNanomaterials (Basel, Switzerland) · 2025
    Article
  5. Article
  6. Encapsulins: catalysis inside a shell.Current opinion in microbiology · 2025
    Review
  7. Article
  8. The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024
    Review
  9. Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024
    Review
  10. Article
  11. Review
  12. Review
  13. Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Structure and heterogeneity of a highly cargo-loaded encapsulin shell.bioRxiv : the preprint server for biology · 2023
    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

10 authors.

Didi HeInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, United Kingdom.ORCID 0000-0002-3360-9352
Sam HughesThe School of Chemistry, The University of Edinburgh, Edinburgh, United Kingdom.
Sally Vanden-HehirThe School of Chemistry, The University of Edinburgh, Edinburgh, United Kingdom.
Atanas GeorgievInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, United Kingdom.
Kirsten AltenbachInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, United Kingdom.
Emma TarrantInstitute for Cell and Molecular Biosciences, Newcastle University, Newcasle upon Tyne, United Kingdom.
C Logan MackayThe School of Chemistry, The University of Edinburgh, Edinburgh, United Kingdom.
Kevin J WaldronInstitute for Cell and Molecular Biosciences, Newcastle University, Newcasle upon Tyne, United Kingdom.ORCID 0000-0002-5577-7357
David J ClarkeThe School of Chemistry, The University of Edinburgh, Edinburgh, United Kingdom.ORCID 0000-0002-3741-2952
Jon Marles-WrightInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, United Kingdom.ORCID 0000-0002-9156-3284

Funding

Biotechnology and Biological Sciences Research Council BB/N005570/1Wellcome TrustWellcome Trust 098375/Z/12/Z
6 · The paper itself

Abstract

Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage. We have characterized the structure and function of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid. We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface. EncFtn adopts an open decameric structure that is topologically distinct from other ferritins. While EncFtn acts as a ferroxidase, it cannot mineralize iron. Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage. This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.

Indexed as

CeruloplasminCrystallography, X-RayFerritinsIronMicroscopy, Electron, TransmissionModels, MolecularProtein ConformationProtein MultimerizationRhodospirillum rubrumCeruloplasminFerritinsIronbiochemistrybiophysicsencapsulated ferritinencapsulinferritinRhodospirillum rubrumstructural biology

Identifiers

PMID27529188
PMCPMC5012862

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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.