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''' | + | {{Structure |
| + | |PDB= 1n51 |SIZE=350|CAPTION= <scene name='initialview01'>1n51</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=ATN:N-[(2S,3R)-3-AMINO-2-HYDROXY-4-PHENYL-BUTANOYL]-L-PROLYL-L-PROLYL-L-ALANINAMIDE'>ATN</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= PEPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Aminopeptidase P in complex with the inhibitor apstatin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1N51 is a [ | + | 1N51 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N51 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15388923 15388923] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: proline specific]] | [[Category: proline specific]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:14 2008'' |
Revision as of 10:52, 20 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | PEPP (Escherichia coli) | ||||||
| Activity: | Xaa-Pro aminopeptidase, with EC number 3.4.11.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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