Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs.

@article{Goffin1998MultimodularPP,
  title={Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs.},
  author={Colette Goffin and J. M. Ghuysen},
  journal={Microbiology and molecular biology reviews : MMBR},
  year={1998},
  volume={62 4},
  pages={1079-93}
}
The monofunctional penicillin-binding DD-peptidases and penicillin-hydrolyzing serine beta-lactamases diverged from a common ancestor by the acquisition of structural changes in the polypeptide chain while retaining the same folding, three-motif amino acid sequence signature, serine-assisted catalytic mechanism, and active-site topology. Fusion events gave rise to multimodular penicillin-binding proteins (PBPs). The acyl serine transferase penicillin-binding (PB) module possesses the three… CONTINUE READING
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