Abstract
THE structure of ferritin is of considerable interest because of its widespread occurrence in higher organisms, signifying a general need to store iron and remove this essential, but toxic element. Horse spleen apoferritin has a molecular weight (MW) of about 444,000 and is composed of 24 subunits (MW 18,500) each containing about 163 amino acids1. These are arranged in 432 symmetry to form a nearly spherical hollow shell with outside and inside diameters approximately 130 Å and 75 Å respectively1–3. The large cavity inside the molecule can store up to 4,500 Fe atoms, packaged in a microcrystalline inorganic component of approximate composition (FeOOH)8 (FeO:OPO3H2) (refs 4–6). The atomic structure of the micro-crystals is not specifically related to the surrounding protein structure6. Apoferritin catalyses the oxidation of Fe(II) which it retains inside the molecule as the ferric hydrolysate7,8. Our 6-Å resolution structure of apoferritin3 showed the presence of several rods of electron density, tentatively assigned as α helices, and channels passing through the shell, which could provide an access route for Fe atoms. These features have been confirmed at 2.8-Å resolution and we can now also provide a plausible subunit conformation and quaternary structure.
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References
Harrison, P. M. Seminars Haematol. 14, 55–70 (1977).
Harrison, P. M., Hoare, R. J., Hoy, T. G. & Macara, I. G. in Iron in Biochemistry and Medicine (eds Jacobs, A. & Worwood, M.) 73–114 (Academic New York and London, 1974).
Hoare, R. J., Harrison, P. M. & Hoy, T. G. Nature 255, 653–654 (1975).
Massover, W. H. & Cowley, J. M. Proc. natn. Acad. Sci. U.S.A. 70, 3847–3851 (1973).
Granick, S. Chem. Rev. 38, 379–403 (1946).
Fischbach, F. A., Harrison, P. M. & Hoy, T. G. J. molec. Biol. 39, 235–238 (1969).
Niederer, W. Experientia 26, 218–220 (1970).
Macara, I. G., Hoy, T. G. & Harrison, P. M. Biochem. J. 126, 151–162 (1972).
Blow, D. M. & Crick, F. H. C. Acta crystallogr. 12, 794–802 (1959).
North, A. C. T. Acta Crystallogr. 18, 212–216 (1965).
Niitsu, Y., Ishitani, K. & Listowsky, I. Biochem. biophys. Res. Commun. 55, 1134–1140 (1973).
Ishitani, K., Niitsu, Y. & Listowsky, I. J. biol. Chem. 250, 3142–3148 (1975).
Hendrickson, W. A., Klippenstein, G. L. & Ward, K. B. Proc. natn. Acad. Sci. U.S.A. 72, 2160–2164 (1975).
Champness, J. N., Bloomer, A. C., Bricogne, G., Butler, P. J. G. & Klug, A. Nature 259, 20–24 (1976).
Treffry, A., Banyard, S. H., Hoare, R. J. & Harrison, P. M. in Proteins of Iron Metabolism (eds Brown, E. B., Aisen, P., Fielding, J. & Crichton, R. R.) 3–11 (Grune and Stratton, New York, San Francisco and London, 1977).
Stenkamp, R. E., Sieker, L. C. & Jensen, L. H. J. molec. Biol. 100, 23–34 (1976).
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BANYARD, S., STAMMERS, D. & HARRISON, P. Electron density map of apoferritin at 2.8-Å resolution. Nature 271, 282–284 (1978). https://doi.org/10.1038/271282a0
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DOI: https://doi.org/10.1038/271282a0
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