PMID:2190093
| Citation |
Nordlund, P, Sjöberg, BM and Eklund, H (1990) Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345:593-8 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1038/345593a0 |
| Keywords |
Amino Acid Sequence; Animals; Binding Sites; Crystallization; Escherichia coli/analysis; Free Radicals; Hemerythrin; Iron; Macromolecular Substances; Molecular Sequence Data; Molecular Structure; Protein Conformation; Proteins; Ribonucleotide Reductases; Sequence Homology, Nucleic Acid; Tyrosine |
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