Uppsten, Malin
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Abstract
Ribonucleotide reductase is an indispensable enzyme for all cells, since it catalyses the biosynthesis of the precursors necessary for both building and repairing DNA. The ribonucleotide reductase class I enzymes, present in all mammals as well as in many prokaryotes and DNA viruses, are composed mostly of two homodimeric proteins, R1 and R2. The reaction involves long-range radical transfer between the two proteins. Here, we present the first crystal structure of a ribonucleotide reductase R1/R2 holocomplex. The biological relevance of this complex is based on the binding of the R2 C terminus in the hydrophobic cleft of R1, an interaction proven to be crucial for enzyme activity, and by the fact that all conserved amino acid residues in R2 are facing the R1 active sites. We suggest that the asymmetric R1/R2 complex observed in the 4 A crystal structure of Salmonella typhimurium ribonucleotide reductase represents an intermediate stage in the reaction cycle, and at the moment of reaction the homodimers transiently form a tight symmetric complex. (c) 2006 Elsevier Ltd. All rights reserved.
Keywords
ribonucleotide reductase; RNR; holocomplex; crystal structure; R2 C terminus
Published in
Journal of Molecular Biology
2006, volume: 359, number: 2, pages: 365-377
Publisher: ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
SLU Authors
Uhlin, Ulla
- Department of Molecular Biology, Swedish University of Agricultural Sciences
- Department of Molecular Biology, Swedish University of Agricultural Sciences
UKÄ Subject classification
Bioprocess Technology
Publication identifier
- DOI: https://doi.org/10.1016/j.jmb.2006.03.035
Permanent link to this page (URI)
https://res.slu.se/id/publ/9282