Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.

@article{Nauton2008StructuralII,
  title={Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.},
  author={Lionel Nauton and Richard Kahn and Gianpiero Garau and Jorge F Hernandez and Otto Dideberg},
  journal={Journal of molecular biology},
  year={2008},
  volume={375 1},
  pages={257-69}
}
One mechanism by which bacteria can escape the action of beta-lactam antibiotics is the production of metallo-beta-lactamases. Inhibition of these enzymes should restore the action of these widely used antibiotics. The tetrameric enzyme L1 from Stenotrophomonas maltophilia was used as a model system to determine a series of high-resolution crystal structures of apo, mono and bi-metal substituted proteins as well as protein-inhibitor complexes. Unexpectedly, although the apo structure revealed… CONTINUE READING