Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics.

@article{Kishida2006CrystalSO,
  title={Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics.},
  author={Hiroyuki Kishida and Satoru Unzai and David I Roper and Adrian Lloyd and S -J Park and Jeremy R.H. Tame},
  journal={Biochemistry},
  year={2006},
  volume={45 3},
  pages={783-92}
}
The crystal structure of penicillin binding protein 4 (PBP4) from Escherichia coli, which has both DD-endopeptidase and DD-carboxypeptidase activity, is presented. PBP4 is one of 12 penicillin binding proteins in E. coli involved in the synthesis and maintenance of the cell wall. The model contains a penicillin binding domain similar to known structures, but includes a large insertion which folds into domains with unique folds. The structures of the protein covalently attached to five different… CONTINUE READING