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A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase
Author(s) -
Derek T. Logan,
Etienne Mulliez,
Karl-Magnus Larsson,
Sabrina Bodevin,
Mohamed Atta,
Pierre E. Garnaud,
BrittMarie Sjöberg,
Marc Fontecave
Publication year - 2003
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0736456100
Subject(s) - ribonucleotide reductase , rubredoxin , protein subunit , escherichia coli , chemistry , binding site , active site , enzyme , mutant , biochemistry , oxidoreductase , stereochemistry , biology , gene
A Zn(Cys)(4) center has been found in the C-terminal region of the crystal structure of the anaerobic class III ribonucleotide reductase (RNR) from bacteriophage T4. The metal center is structurally related to the zinc ribbon motif and to rubredoxin and rubrerythrin. Mutant enzymes of the homologous RNR from Escherichia coli, in which the coordinating cysteines, conserved in almost all known class III RNR sequences, have been mutated into alanines, are shown to be inactive as the result of their inability to generate the catalytically essential glycyl radical. The possible roles of the metal center are discussed in relationship to the currently proposed reaction mechanism for generation of the glycyl radical in class III RNRs.

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