The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2.

@article{Kauppi1996TheTS,
  title={The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2.},
  author={B Kauppi and B B Nielsen and Subramanyan Ramaswamy and Ingrid Kj\oller Larsen and Michael W. Thelander and Lars Thelander and Hans Eklund},
  journal={Journal of molecular biology},
  year={1996},
  volume={262 5},
  pages={706-20}
}
The three-dimensional structure of mouse ribonucleotide reductase R2 has been determined at 2.3 A resolution using molecular replacement and refined to an R-value of 19.1% (Rfree = 25%) with good stereo-chemistry. The overall tertiary structure architecture of mouse R2 is similar to that from Escherichia coli R2. However, several important structural differences are observed. Unlike the E. coli protein, the mouse dimer is completely devoid of beta-strands. The sequences differ significantly… CONTINUE READING
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