Crystal structure of human homogentisate dioxygenase

@article{Titus2000CrystalSO,
  title={Crystal structure of human homogentisate dioxygenase},
  author={Greg P. Titus and Heather A. Mueller and John W. Burgner and Santiago Rodrı́guez de C{\'o}rdoba and Miguel A. Pe{\~n}alva and David E. Timm},
  journal={Nature Structural Biology},
  year={2000},
  volume={7},
  pages={542-546}
}
Homogentisate dioxygenase (HGO) cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. HGO deficiency causes alkaptonuria (AKU), the first human disease shown to be inherited as a recessive Mendelian trait. Crystal structures of apo-HGO and HGO containing an iron ion have been determined at 1.9 and 2.3 Å resolution, respectively. The HGO protomer, which contains a 280-residue N-terminal domain and a 140-residue C-terminal domain, associates as a hexamer arranged as a dimer… 

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