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Three-dimensional structure of the free radical protein of ribonucleotide reductase

Nature volume 345, pages 593–598 (1990)Cite this article

Abstract

The enzyme ribonucleotide reductase furnishes precursors for the DNA synthesis of all living cells. One of its constituents, the free radical protein, has an unusual α-helical structure. There are two iron centres that are about 25 Å apart in the dimeric molecule. Tyrosine 122, which harbours the stable free radical necessary for the activity of ribonucleotide reductase, is buried inside the protein and is located 5 Å from the closest iron atom.

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Author notes

  1. Britt-Marie Sjöberg: Department of Molecular Biology, University of Stockholm, S-10691 Stockholm, Sweden

Authors and Affiliations

  1. Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Center, Box 590, S-75124, Uppsala, Sweden

    Pär Nordlund, Britt-Marie Sjöberg & Hans Eklund

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  1. Pär Nordlund
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  2. Britt-Marie Sjöberg
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  3. Hans Eklund
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Nordlund, P., Sjöberg, BM. & Eklund, H. Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345, 593–598 (1990). https://doi.org/10.1038/345593a0

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