Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site.

@article{Li2007CrystalSO,
  title={Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site.},
  author={Sheng Li and Yongcheng Lu and Baozhen Peng and Jianping Ding},
  journal={The Biochemical journal},
  year={2007},
  volume={401 1},
  pages={39-47}
}
PRPP (phosphoribosylpyrophosphate) is an important metabolite essential for nucleotide synthesis and PRS (PRPP synthetase) catalyses synthesis of PRPP from R5P (ribose 5-phosphate) and ATP. The enzymatic activity of PRS is regulated by phosphate ions, divalent metal cations and ADP. In the present study we report the crystal structures of recombinant human PRS1 in complexes with SO4(2-) ions alone and with ATP, Cd2+ and SO4(2-) ions respectively. The AMP moiety of ATP binds at the ATP-binding… CONTINUE READING
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