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Three-dimensional structure of the free radical protein of ribonucleotide reductase
P Nordlund1, B M Sjöberg, H Eklund
1Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
Nature
|June 14, 1990
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 alpha-helical structure. There are two iron centres that are about 25 A 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 A from the closest iron atom.