Identification of the stable free radical tyrosine residue in ribonucleotide reductase. A sequence comparison

B. M. Sjöberg, H. Eklund, J. A. Fuchs, J. Carlson, N. M. Standart, J. V. Ruderman, S. J. Bray, T. Hunt

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

The small subunit of ribonucleoside diphosphate reductase contains a unique tyrosine radical and a bi-nuclear iron center. An alignment of different primary structures of the small subunit in Escherichia coli, the marine mollusc Spisula solidissima, Epstein Barr and Herpes simplex viruses shows that regions comprising residues 115-122, 204-212 and 234-241 (in E.coli numbering) are strikingly similar and are likely to be recognized as functionally important. Two of 16 tyrosine residues and 2 of 8 histidine residues are conserved. We propose that Tyr-122 is responsible for radical stabilization and that His-118 and His-241 together with Glu-115 and Asp-237 or Glu-238 are ligands of the iron center. Ribonucleotide reductase Secondary structure prediction Sequence comparison Tyrosine radical.

Original languageEnglish (US)
Pages (from-to)99-102
Number of pages4
JournalFEBS Letters
Volume183
Issue number1
DOIs
StatePublished - Apr 8 1985
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics
  • Molecular Biology
  • Biophysics
  • Structural Biology
  • Biochemistry
  • Cell Biology

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