Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.

@article{Larsen1999ThreedimensionalSO,
  title={Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.},
  author={T. M. Larsen and S. Boehlein and S. Schuster and N. Richards and J. Thoden and H. Holden and I. Rayment},
  journal={Biochemistry},
  year={1999},
  volume={38 49},
  pages={
          16146-57
        }
}
Asparagine synthetase B catalyzes the assembly of asparagine from aspartate, Mg(2+)ATP, and glutamine. Here, we describe the three-dimensional structure of the enzyme from Escherichia colidetermined and refined to 2.0 A resolution. Protein employed for this study was that of a site-directed mutant protein, Cys1Ala. Large crystals were grown in the presence of both glutamine and AMP. Each subunit of the dimeric protein folds into two distinct domains. The N-terminal region contains two layers of… Expand
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The three-dimensional structure of carbamoyl phosphate synthetase from E. coli refined to 2.1 A resolution with an R factor of 17.9% is described and it is shown that the enzyme is an alpha,beta-heterodimer consisting of a small sub unit that hydrolyzes glutamine and a large subunit that catalyzes the two required phosphorylation events. Expand
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