Structure of ribonucleotide reductase protein R1

Nature. 1994 Aug 18;370(6490):533-9. doi: 10.1038/370533a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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


  • Peptide Fragments
  • Ribonucleotide Reductases
  • Cysteine