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1n51

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[[Image:1n51.gif|left|200px]]
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{{STRUCTURE_1n51| PDB=1n51 | SCENE= }}
{{STRUCTURE_1n51| PDB=1n51 | SCENE= }}
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'''Aminopeptidase P in complex with the inhibitor apstatin'''
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===Aminopeptidase P in complex with the inhibitor apstatin===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15388923 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15388923}}
==About this Structure==
==About this Structure==
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[[Category: Manganese enzyme]]
[[Category: Manganese enzyme]]
[[Category: Proline specific]]
[[Category: Proline specific]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:06:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:58:54 2008''

Revision as of 01:58, 28 July 2008

Template:STRUCTURE 1n51

Aminopeptidase P in complex with the inhibitor apstatin

Template:ABSTRACT PUBMED 15388923

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

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