Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin.

@article{Graham2004StructureOE,
  title={Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin.},
  author={Stephen C. Graham and Megan Maher and William Harold Michael Garth Simmons and Hans C. Freeman and J Mitchell Guss},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2004},
  volume={60 Pt 10},
  pages={1770-9}
}
Aminopeptidase P (APPro) is a metalloprotease whose active site includes a dinuclear manganese(II) cluster. The enzyme cleaves the N-terminal residue from a polypeptide when the second residue is proline. A complex of Escherichia coli APPro (EcAPPro) with an inhibitor, apstatin [N-(2S,3R)-3-amino-2-hydroxy-4-phenyl-butanoyl-L-prolyl-L-prolyl-L-alaninamide], has been crystallized. Apstatin binds to the active site of EcAPPro with its N-terminal amino group coordinated to one of the two Mn(II… CONTINUE READING
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