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The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site

Nature Structural Biology volume 7, pages 38–43 (2000)Cite this article

Abstract

Ferritin is characterized by a highly conserved architecture that comprises 24 subunits assembled into a spherical cage with 432 symmetry. The only known exception is the dodecameric ferritin from Listeria innocua. The structure of Listeria ferritin has been determined to a resolution of 2.35 Å by molecular replacement, using as a search model the structure of Dps from Escherichia coli. The Listeria 12-mer is endowed with 23 symmetry and displays the functionally relevant structural features of the ferritin 24-mer, namely the negatively charged channels along the three-fold symmetry axes that serve for iron entry into the cavity and a negatively charged internal cavity for iron deposition. The electron density map shows 12 iron ions on the inner surface of the hollow core, at the interface between monomers related by two-fold axes. Analysis of the nature and stereochemistry of the iron-binding ligands reveals strong similarities with known ferroxidase sites. The L. innocua ferritin site, however, is the first described so far that has ligands belonging to two different subunits and is not contained within a four-helix bundle.

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Figure 1: Monomer fold of L. innocua ferritin and comparison with related structures.
Figure 2: Structural alignment of the L. innocua ferritin, E. coli Dps and horse spleen L-chain sequences.
Figure 3: View of L. innocua ferritin along the 'ferritin-like' interface at the three-fold axis.
Figure 4: Iron-binding site in L. innocua ferritin in comparison with proven ferroxidase sites.

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Acknowledgements

This work was supported in part by grants from the Istituto Pasteur-Fondazione Cenci Bolognetti and the Agenzia Spaziale Italiana (to D.T.) and from the Ministero per l'Università e Ricerca Scientifica e Tecnologica, Progetto Biologia Strutturale (to E.C. and D.T.). The authors are grateful to M. Bozzi for providing the purified protein, to P. Kanellopoulos for data measurement at DESY and to M. Rizzi for continuous help and fruitful discussions.

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Authors and Affiliations

  1. Department of Biochemical Sciences "A. Rossi Fanelli", CNR Center of Molecular Biology, University La Sapienza, Piazzale Aldo Moro 5, Rome, 00185, Italy

    Andrea Ilari, Simonetta Stefanini, Emilia Chiancone & Demetrius Tsernoglou

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  1. Andrea Ilari
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  2. Simonetta Stefanini
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  3. Emilia Chiancone
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  4. Demetrius Tsernoglou
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Correspondence to Emilia Chiancone.

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Ilari, A., Stefanini, S., Chiancone, E. et al. The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nat Struct Mol Biol 7, 38–43 (2000). https://doi.org/10.1038/71236

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