1n51
From Proteopedia
(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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| - | [[Image:1n51.gif|left|200px]]<br /><applet load="1n51" size=" | + | [[Image:1n51.gif|left|200px]]<br /><applet load="1n51" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n51, resolution 2.30Å" /> | caption="1n51, resolution 2.30Å" /> | ||
'''Aminopeptidase P in complex with the inhibitor apstatin'''<br /> | '''Aminopeptidase P in complex with the inhibitor apstatin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Aminopeptidase P (APPro) is a metalloprotease whose active site includes a | + | 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== | ==About this Structure== | ||
| - | 1N51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN and ATN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Full crystallographic information is available from [http:// | + | 1N51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=ATN:'>ATN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N51 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xaa-Pro aminopeptidase]] | [[Category: Xaa-Pro aminopeptidase]] | ||
| - | [[Category: Freeman, H | + | [[Category: Freeman, H C.]] |
| - | [[Category: Graham, S | + | [[Category: Graham, S C.]] |
| - | [[Category: Guss, J | + | [[Category: Guss, J M.]] |
| - | [[Category: Lee, M | + | [[Category: Lee, M H.]] |
| - | [[Category: Maher, M | + | [[Category: Maher, M J.]] |
| - | [[Category: Simmons, W | + | [[Category: Simmons, W H.]] |
[[Category: ATN]] | [[Category: ATN]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: proline specific]] | [[Category: proline specific]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:20 2008'' |
Revision as of 12:02, 21 February 2008
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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 and 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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