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={J. Thoden and G. Phillips and T. Neal and F. Raushel and H. 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… Expand
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The structure of human erythrocytic carbonic anhydrase II has been refined by constrained and restrained structure–factor least‐squares refinement at 2.0 Å resolution and some of the hydrogen bond donor–acceptor relations in the active site can be assigned. Expand
Biochemistry
The Department of Biochemistry is internationally recognized for its research and education and offers a world-class interdisciplinary research environment in a beautiful mountain setting. As part ofExpand
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