PMID:8052308

Citation	Uhlin, U and Eklund, H (1994) Structure of ribonucleotide reductase protein R1. Nature 370:533-9
Abstract	Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribonucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteins. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl end in a flexible arm. The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction.
Links	PubMed Online version:10.1038/370533a0
Keywords	Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Cysteine; Escherichia coli/enzymology; Models, Chemical; Models, Molecular; Molecular Sequence Data; Peptide Fragments/metabolism; Protein Conformation; Protein Structure, Secondary; Ribonucleotide Reductases/chemistry; Ribonucleotide Reductases/metabolism; Sequence Homology, Amino Acid
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