Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.

@article{Schumacher2000CrystalSO,
  title={Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.},
  author={Maria A. Schumacher and Daniel M Scott and Irimpan I Mathews and Steven E. Ealick and David S. Roos and Buddy Ullman and Richard G Brennan},
  journal={Journal of molecular biology},
  year={2000},
  volume={296 2},
  pages={
          549-67
        }
}
Adenosine kinase (AK) is a key purine metabolic enzyme from the opportunistic parasitic protozoan Toxoplasma gondii and belongs to the family of carbohydrate kinases that includes ribokinase. To understand the catalytic mechanism of AK, we determined the structures of the T. gondii apo AK, AK:adenosine complex and the AK:adenosine:AMP-PCP complex to 2.55 A, 2.50 A and 1.71 A resolution, respectively. These structures reveal a novel catalytic mechanism that involves an adenosine-induced domain… CONTINUE READING
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