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Structure, function, and mechanism of ribonucleotide reductases
Matthias Kolberg1, Kari R Strand, Pål Graff
1Department of Molecular Biosciences, University of Oslo, P.O. Box 1041, Blindern, NO-0316 Oslo, Norway.
Biochimica Et Biophysica Acta
|May 26, 2004
Summary
Ribonucleotide reductase (RNR) enzymes, crucial for DNA synthesis and repair, show conserved active sites across classes despite diverse cofactors. Structural studies reveal evolutionary links and mechanistic insights into these vital proteins.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Ribonucleotide reductase (RNR) synthesizes deoxynucleotides essential for DNA synthesis and repair.
- Recent crystal structures illuminate the subunits of all three RNR classes.
- RNRs are model systems for diverse protein families due to varied cofactors.
Purpose of the Study:
- To review recent structural and spectroscopic studies of RNRs.
- To provide deeper insight into RNR mechanistic properties, evolutionary relationships, and diversity.
- To compare diiron centers in Class I RNR R2 proteins from mouse and E. coli.
Main Methods:
- Structural analysis of RNR protein subunits.
- Spectroscopic studies of RNR mechanisms.
- Comparative analysis of R2 protein structures.
Main Results:
- All RNR classes share a conserved active site cysteine residue, suggesting a common evolutionary origin.
- Structural and functional similarities indicate RNRs evolved from a common ancestral reductase.
- Class I RNR R2 proteins exhibit dynamic shifts and cooperative metal binding; yeast RNR shows unique heterodimerization.
Conclusions:
- RNRs, despite cofactor diversity, share mechanistic and structural similarities, pointing to a common ancestor.
- RNR's role in DNA synthesis makes it a key target for cell growth control.
- New structural data enhances understanding of RNR diversity, mechanisms, and cell cycle roles.