Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad.

@article{Hung2007CrystalSO,
  title={Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad.},
  author={Chiu-Lien Hung and Jia-Hsin Liu and Wei-Chun Chiu and Shao-Wei Huang and Jenn-Kang Hwang and Wen-Ching Wang},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 16},
  pages={12220-9}
}
Helicobacter pylori AmiF formamidase that hydrolyzes formamide to produce formic acid and ammonia belongs to a member of the nitrilase superfamily. The crystal structure of AmiF was solved to 1.75A resolution using single-wavelength anomalous dispersion methods. The structure consists of a homohexamer related by 3-fold symmetry in which each subunit has an alpha-beta-beta-alpha four-layer architecture characteristic of the nitrilase superfamily. One exterior alpha layer faces the solvent… CONTINUE READING