A metal binding site in the catalytic subunit of anaerobic ribonucleotide reductase.
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/128496
- author
- Logan, Derek LU ; Mulliez, E ; Larsson., K-M ; Bodevin, S ; Atta, M ; Garnaud, P E ; Sjöberg, B-M and Fontecave, M
- organization
- publishing date
- 2003
- 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 Academy of Sciences
- external identifiers
-
- pmid:12655046
- wos:000182058400054
- scopus:0037389527
- ISSN
- 1091-6490
- DOI
- 10.1073/pnas.0736456100
- language
- English
- LU publication?
- yes
- id
- 7c6128c0-083c-4cf0-a3a7-15f7110f1361 (old id 128496)
- date added to LUP
- 2016-04-01 12:10:27
- date last changed
- 2022-01-26 23:53:02
@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 Academy of 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/10.1073/pnas.0736456100}}, doi = {{10.1073/pnas.0736456100}}, volume = {{100}}, year = {{2003}}, }