A glycyl radical site in the crystal structure of a class III ribonucleotide reductase |
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Authors: | Logan D T Andersson J Sjöberg B M Nordlund P |
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Institution: | Department of Biochemistry and Department of Molecular Biology, Stockholm University, S-106 91 Stockholm, Sweden. derek@biokemi.su.se |
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Abstract: | Ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides. Three classes have been identified, all using free-radical chemistry but based on different cofactors. Classes I and II have been shown to be evolutionarily related, whereas the origin of anaerobic class III has remained elusive. The structure of a class III enzyme suggests a common origin for the three classes but shows differences in the active site that can be understood on the basis of the radical-initiation system and source of reductive electrons, as well as a unique protein glycyl radical site. A possible evolutionary relationship between early deoxyribonucleotide metabolism and primary anaerobic metabolism is suggested. |
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