title: Structure of ribonucleotide reductase protein R1.
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.
authors.affiliation: Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
authors.forename: U
authors.initials: U
authors.lastname: Uhlin
authors.forename: H
authors.initials: H
authors.lastname: Eklund
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D003545:Cysteine; D004926:Escherichia coli / Q000201:enzymology; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012264:Ribonucleotide Reductases / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D010446:Peptide Fragments; D012264:Ribonucleotide Reductases; D003545:Cysteine