Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor

@article{Paetzel1998CrystalSO,
  title={Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor},
  author={Mark Paetzel and Ross E. Dalbey and Natalie C. J. Strynadka},
  journal={Nature},
  year={1998},
  volume={396},
  pages={186-190}
}
The signal peptidase (SPase) from Escherichia coli is a membrane-bound endopeptidase with two amino-terminal transmembrane segments and a carboxy-terminal catalytic region which resides in the periplasmic space. SPase functions to release proteins that have been translocated into the inner membrane from the cell interior, by cleaving off their signal peptides. We report here the X-ray crystal structure of a catalytically active soluble fragment of E. coli SPase (SPase Δ2–75),. We have… CONTINUE READING

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