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1n51
From Proteopedia
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[[Image:1n51.gif|left|200px]] | [[Image:1n51.gif|left|200px]] | ||
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'''Aminopeptidase P in complex with the inhibitor apstatin''' | '''Aminopeptidase P in complex with the inhibitor apstatin''' | ||
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[[Category: Maher, M J.]] | [[Category: Maher, M J.]] | ||
[[Category: Simmons, W H.]] | [[Category: Simmons, W H.]] | ||
| - | [[Category: | + | [[Category: Aminopeptidase]] |
| - | [[Category: | + | [[Category: Inhibitor complex]] |
| - | [[Category: | + | [[Category: Manganese enzyme]] |
| - | [[Category: | + | [[Category: Proline specific]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:06:15 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:06, 2 May 2008
Aminopeptidase P in complex with the inhibitor apstatin
Overview
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-alanina mide], 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 cleft. The structure of the apstatin-EcAPPro complex has been refined at 2.3 A resolution with residuals R = 0.179 and R(free) = 0.204. The structure of the complex illustrates how apstatin inhibits APPro and suggests how substrates may bind to the enzyme, but the basis of the proline-specificity remains elusive.
About this Structure
1N51 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin., Graham SC, Maher MJ, Simmons WH, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1770-9. Epub 2004, Sep 23. PMID:15388923 Page seeded by OCA on Sat May 3 02:06:15 2008
