A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem.

@article{Garau2005AME,
  title={A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem.},
  author={Gianpiero Garau and Carine Bebrone and Christine Anne and Moreno Galleni and J J Frere and Otto Dideberg},
  journal={Journal of molecular biology},
  year={2005},
  volume={345 4},
  pages={785-95}
}
One strategy developed by bacteria to resist the action of beta-lactam antibiotics is the expression of metallo-beta-lactamases. CphA from Aeromonas hydrophila is a member of a clinically important subclass of metallo-beta-lactamases that have only one zinc ion in their active site and for which no structure is available. The crystal structures of wild-type CphA and its N220G mutant show the structural features of the active site of this enzyme, which is modeled specifically for carbapenem… CONTINUE READING

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