The structure and function of Escherichia coli penicillin-binding protein 3

@article{NguyenDistche1998TheSA,
  title={The structure and function of Escherichia coli penicillin-binding protein 3},
  author={Martine Nguyen-Dist{\`e}che and Claudine Fraipont and Nienke Buddelmeijer and Nanne Nanninga},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={1998},
  volume={54},
  pages={309-316}
}
Escherichia coli penicillin-binding protein PBP3 is a key element in cell septation. It is presumed to catalyse a transpeptidation reaction during biosynthesis of the septum peptidoglycan but, in vitro, its enzymatic activity has only been demonstrated with thiolester analogues of the natural peptide substrate. It has no detectable transglycosylase activity with lipid II as substrate. This tripartite protein is constructed of an N-terminal membrane anchor-containing module that is essential for… CONTINUE READING

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