ArticleProceedings of the National Academy of Sciences of the United States of America2001
Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 57 citations in OpenAlex.
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- Hydrogen bond network between amino acid radical intermediates on the proton-coupled electron transfer pathway of E. coli α2 ribonucleotide reductase.Journal of the American Chemical Society · 2015Article
- Choosing the right metal: case studies of class I ribonucleotide reductases.The Journal of biological chemistry · 2014Review
- Conserved electron donor complex Dre2-Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A novel clade of unique eukaryotic ribonucleotide reductase R2 subunits is exclusive to apicomplexan parasites.Journal of molecular evolution · 2013Article
- Regulation of ribonucleotide reductase in response to iron deficiency.Molecular cell · 2011Article
- Investigation of in vivo diferric tyrosyl radical formation in Saccharomyces cerevisiae Rnr2 protein: requirement of Rnr4 and contribution of Grx3/4 AND Dre2 proteins.The Journal of biological chemistry · 2011Article
- Ribosome synthesis-unrelated functions of the preribosomal factor Rrp12 in cell cycle progression and the DNA damage response.Molecular and cellular biology · 2011Article
- Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization.Nature structural & molecular biology · 2011Article
- Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.Annual review of biochemistry · 2011Review
- Highly mutagenic and severely imbalanced dNTP pools can escape detection by the S-phase checkpoint.Nucleic acids research · 2010Article
- Expression, purification, crystallization and preliminary X-ray analysis of ORF60, the small subunit (R2) of ribonucleotide reductase from Kaposi's sarcoma-associated herpesvirus (KSHV).Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- In silico evidence for functional specialization after genome duplication in yeast.FEMS yeast research · 2009Article
- Dif1 controls subcellular localization of ribonucleotide reductase by mediating nuclear import of the R2 subunit.Molecular and cellular biology · 2008Article
- The metal centres of particulate methane mono-oxygenase.Biochemical Society transactions · 2008Review
- Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase.Molecular cell · 2008Article
- Determination of the in vivo stoichiometry of tyrosyl radical per betabeta' in Saccharomyces cerevisiae ribonucleotide reductase.Biochemistry · 2006Article
- Article
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5 authors at 2 institutions in 1 country.
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Abstract
The R2 subunits of class I ribonucleotide reductases (RNRs) house a diferric-tyrosyl radical (Y*) cofactor essential for DNA synthesis. In yeast, there are two R2 proteins, Y2 and Y4. Although both Y2 and Y4 are homologous to R2s from other organisms, Y4 lacks three conserved iron-binding residues, and its exact function is unclear. Y4 is required for assembly of the diferric-Y* cofactor in Y2, and the two proteins can form both homodimeric and heterodimeric complexes. The Y2Y4 heterodimer was crystallized from a mixture of the two proteins, and its structure was determined to 2.8 A resolution. Both Y2 and Y4 are completely alpha helical and resemble the mouse and Escherichia coli R2s in overall fold. Three alpha helices not observed in the mouse R2 structure are present at the Y2 N terminus, and one extra N-terminal helix is observed in Y4. In addition, one of the eight principal helices in both Y2 and Y4, alphaD, is shifted significantly from its position in mouse R2. The heterodimer interface is similar to the mouse R2 homodimer interface in size and interacting residues, but loop regions at the interface edges differ. A single metal ion, assigned as Zn(II), occupies the Fe2 position in the Y2 active site. Treatment of the crystals with Fe(II) results in difference electron density consistent with formation of a diiron center. No metal-binding site is observed in Y4. Instead, the residues in the active site region form a hydrogen-bonding network involving an arginine, two glutamic acids, and a water molecule.
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