Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center.

@article{Thoden2001MolecularSO,
  title={Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center.},
  author={James B. Thoden and George N. Phillips and Tess M S Neal and Frank M Raushel and Hazel M Holden},
  journal={Biochemistry},
  year={2001},
  volume={40 24},
  pages={6989-97}
}
Dihydroorotase plays a key role in pyrimidine biosynthesis by catalyzing the reversible interconversion of carbamoyl aspartate to dihydroorotate. Here we describe the three-dimensional structure of dihydroorotase from Escherichia coli determined and refined to 1.7 A resolution. Each subunit of the homodimeric enzyme folds into a "TIM" barrel motif with eight strands of parallel beta-sheet flanked on the outer surface by alpha-helices. Unexpectedly, each subunit contains a binuclear zinc center… CONTINUE READING
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