Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex.

@article{Betts1994CytidineDT,
  title={Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex.},
  author={Laurie Betts and Shuhuai Xiang and Steven A. Short and Richard Wolfenden and Charles W. Carter},
  journal={Journal of molecular biology},
  year={1994},
  volume={235 2},
  pages={635-56}
}
We have solved the structure of Escherichia coli cytidine deaminase (CDA) complexed to the transition state analog, 5-fluoroprimidin-2-one riboside. The monomer of the alpha 2 CDA dimer is composed of a small N-terminal alpha-helical domain with no obvious connection to the active sites, and two, larger, core domains. The two core domains have nearly identical tertiary structures and are related by approximate 2-fold symmetry, but lack internal amino acid sequence homology. Comparison of the… CONTINUE READING