Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion.

@article{Bacik2012ActiveSP,
  title={Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion.},
  author={John-Paul Bacik and Garrett E. Whitworth and Keith A Stubbs and David J Vocadlo and Brian L Mark},
  journal={Chemistry & biology},
  year={2012},
  volume={19 11},
  pages={1471-82}
}
NagZ is a glycoside hydrolase that participates in peptidoglycan (PG) recycling by removing β-N-acetylglucosamine from PG fragments that are excised from the bacterial cell wall during growth. Notably, the products formed by NagZ, 1,6-anhydroMurNAc-peptides, activate β-lactam resistance in many Gram-negative bacteria, making this enzyme of interest as a potential therapeutic target. Crystal structure determinations of NagZ from Salmonella typhimurium and Bacillus subtilis in complex with… CONTINUE READING