Journal article

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

SC Graham, MJ Maher, WH Simmons, HC Freeman, JM Guss

Acta Crystallographica Section D, Structural Biology | INT UNION CRYSTALLOGRAPHY | Published : 2004


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) atoms at the metal centre. The apstatin hydroxyl group replaces a hydroxide ion which bridges the two metal atoms in the native enzyme. The first proline residue of apstatin lies in a small hydrophobic c..

View full abstract

University of Melbourne Researchers