Cited by 777Iron Metabolism and DisordersEnzyme Structure and FunctionProtein Structure and Dynamics

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Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts

Lawson, David M., Artymiuk, Peter J., Yewdall, Stephen J., Smith, John M. A., Livingstone, J. Craig, Treffry, Amyra, Luzzago, Alessandra, Levi, Sonia, Arosio, Paolo, Cesareni, Gianni, Thomas, Christopher D., Shaw, William V., Harrison, Pauline M.·1991·Nature

DOI 10.1038/349541a0

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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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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: Smith, John M. A.
Levi, Sonia
Arosio, Paolo
Cesareni, Gianni
Thomas, Christopher D.
Shaw, William V.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1991-02
Volume: 349
Issue: 6309
Pages: 541-544
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/349541a0
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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Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts

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