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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5407
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pubmed:dateCreated |
1999-4-13
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1499-504
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:10066165-Acetyltransferases,
pubmed-meshheading:10066165-Amino Acid Sequence,
pubmed-meshheading:10066165-Anaerobiosis,
pubmed-meshheading:10066165-Binding Sites,
pubmed-meshheading:10066165-Crystallography, X-Ray,
pubmed-meshheading:10066165-Dimerization,
pubmed-meshheading:10066165-Evolution, Molecular,
pubmed-meshheading:10066165-Glycine,
pubmed-meshheading:10066165-Hydrogen Bonding,
pubmed-meshheading:10066165-Models, Molecular,
pubmed-meshheading:10066165-Molecular Sequence Data,
pubmed-meshheading:10066165-Mutation,
pubmed-meshheading:10066165-Protein Conformation,
pubmed-meshheading:10066165-Protein Folding,
pubmed-meshheading:10066165-Protein Structure, Secondary,
pubmed-meshheading:10066165-Ribonucleotide Reductases,
pubmed-meshheading:10066165-Viral Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
A glycyl radical site in the crystal structure of a class III ribonucleotide reductase.
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pubmed:affiliation |
Department of Biochemistry and Department of Molecular Biology, Stockholm University, S-106 91 Stockholm, Sweden. derek@biokemi.su.se
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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