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Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
Abstract
Ferritin is important in iron homeostasis. Its twenty-four chains of two types, H and L, assemble as a hollow shell providing an iron-storage cavity. Ferritin molecules in cells containing high levels of iron tend to be rich in L chains, and may have a long-term storage function, whereas H-rich ferritins are more active in iron metabolism. The molecular basis for the greater activity of H-rich ferritins has until now been obscure, largely because the structure of H-chain ferritin has remained unknown owing to the difficulties in obtaining crystals ordered enough for X-ray crystallographic analysis. Here we report the three-dimensional structure of a human ferritin H-chain homopolymer. By genetically engineering a change in the sequence of the intermolecular contact region, we obtained crystals isomorphous with the homologous rat L ferritin and of high enough quality for X-ray diffraction analysis. The X-ray structure of human H ferritin shows a novel metal site embedded within each of its four-helix bundles and we suggest that ferroxidase activity associated with this site accounts for its rapid uptake of iron.
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“Iron from the LIP which is not used for metabolic processes is stored in the cytosol in the “ferritin nano-cage,” a cytosolic heteropolymer composed of 24 subunits of heavy (FTH1) and light (FTL1) ferritin chains (Lawson et al., 1991; Figure 1).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Lawson et al., 1991
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“At the other end of the spectrum, excess iron concentrations are particularly harmful because the highly oxidative microenvironment of the brain lends itself to the production of ROS (180).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [180]
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Metadata
- Authors
- Lawson, D. M., Artymiuk, P. J., Yewdall, S. J., Smith, J. M. A., Livingstone, J. C., Treffry, A., Luzzago, A., Levi, S., Arosio, P., Cesareni, G., Thomas, C. D., Shaw, W. V., & Harrison, P. M.
- Affiliations
- University of Sheffield (GB)
- European Molecular Biology Laboratory (DE)
- University of Milan (IT)
- University of Rome Tor Vergata (IT)
- University of Leicester (GB)
- ORCID
- Venue
- Nature
- Published
- 1991-02
- Volume
- 349
- Issue
- 6309
- Pages
- 541-544
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2108816504
- Cited by
- 777
- References
- 28
- Citations by year
- 2026: 18 · 2025: 21 · 2024: 19 · 2023: 22 · 2022: 20 · 2021: 27 · 2020: 25 · 2019: 19 · 2018: 21 · 2017: 28 · 2016: 22 · 2015: 21 · 2014: 30 · 2013: 30 · 2012: 26
- FWCI
- 19.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Cineca Institutional Research Information System (Tor Vergata University) (submittedVersion)
- Archivio Istituzionale della Ricerca - Università Vita-Salute San Raffaele (submittedVersion)
- Funders
- Wellcome Trust
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- iron homeostasis, iron storage, ferroxidase activity, isomorphous crystals, four-helix bundle, metal sites, iron absorption
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Computer Graphics, Crystallography, Ferritins, Humans, Iron, Models, Molecular, Molecular Sequence Data, Molecular Weight, Recombinant Proteins, X-Ray Diffraction, Rats
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