Structure of ribonucleotide reductase protein R1
Copyright policy )Structure of ribonucleotide reductase protein R1
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.
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Crystallography, X-Ray, Peptide Fragments, Protein Structure, Secondary, Models, Chemical, Ribonucleotide Reductases, Escherichia coli, Amino Acid Sequence, Cysteine
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Crystallography, X-Ray, Peptide Fragments, Protein Structure, Secondary, Models, Chemical, Ribonucleotide Reductases, Escherichia coli, Amino Acid Sequence, Cysteine
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