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

Logan, Derek LU ; Mulliez, E; Larsson., K-M; Bodevin, S; Atta, M; Garnaud, P E; Sjöberg, B-M and Fontecave, M (2003) In Proceedings of the National Academy of Sciences 100(7). p.3826-3831
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.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Proceedings of the National Academy of Sciences
volume
100
issue
7
pages
3826 - 3831
publisher
National Acad Sciences
external identifiers
  • pmid:12655046
  • wos:000182058400054
  • scopus:0037389527
ISSN
1091-6490
DOI
language
English
LU publication?
yes
id
7c6128c0-083c-4cf0-a3a7-15f7110f1361 (old id 128496)
date added to LUP
2007-07-09 15:53:23
date last changed
2018-05-29 10:31:29
@article{7c6128c0-083c-4cf0-a3a7-15f7110f1361,
  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.},
  author       = {Logan, Derek and Mulliez, E and Larsson., K-M and Bodevin, S and Atta, M and Garnaud, P E and Sjöberg, B-M and Fontecave, M},
  issn         = {1091-6490},
  language     = {eng},
  number       = {7},
  pages        = {3826--3831},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {A metal binding site in the catalytic subunit of anaerobic ribonucleotide reductase.},
  url          = {http://dx.doi.org/},
  volume       = {100},
  year         = {2003},
}