1n51
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(New page: 200px<br /><applet load="1n51" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n51, resolution 2.30Å" /> '''Aminopeptidase P in ...)
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Revision as of 19:50, 20 November 2007
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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 with MN and ATN as ligands. Active as Xaa-Pro aminopeptidase, with EC number 3.4.11.9 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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