A metal binding site in the catalytic subunit of anaerobic ribonucleotide reductase.

Research output: Contribution to journalArticle

Abstract

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.

Details

Authors
  • Derek Logan
  • E Mulliez
  • K-M Larsson.
  • S Bodevin
  • M Atta
  • P E Garnaud
  • B-M Sjöberg
  • M Fontecave
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences
Original languageEnglish
Pages (from-to)3826-3831
JournalProceedings of the National Academy of Sciences
Volume100
Issue number7
Publication statusPublished - 2003
Publication categoryResearch
Peer-reviewedYes