1m35
From Proteopedia
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| - | [[Image:1m35.gif|left|200px]] | + | [[Image:1m35.gif|left|200px]] |
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| - | '''Aminopeptidase P from Escherichia coli''' | + | {{Structure |
| + | |PDB= 1m35 |SIZE=350|CAPTION= <scene name='initialview01'>1m35</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</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 from Escherichia coli''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1M35 is a [ | + | 1M35 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=1M35 OCA]. |
==Reference== | ==Reference== | ||
| - | An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution., Graham SC, Lee M, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):897-902. Epub 2003, Apr 25. PMID:[http:// | + | An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution., Graham SC, Lee M, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):897-902. Epub 2003, Apr 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12777807 12777807] |
[[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 12:38:19 2008'' |
Revision as of 10:38, 20 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | pepP (Escherichia coli) | ||||||
| Activity: | Xaa-Pro aminopeptidase, with EC number 3.4.11.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Aminopeptidase P from Escherichia coli
Overview
Aminopeptidase P (AMPP) from Escherichia coli cleaves the N-terminal residue from an oligopeptide if the second residue is proline. The active site contains a dinuclear metal centre. Following earlier structural analyses of crystals in space groups P6(4)22 and I4(1)22, the structure of AMPP has been solved and refined in the orthorhombic space group C222(1) at 2.4 A resolution. There are six subunits in the asymmetric unit. These are arranged in two types of tetramer. One tetramer comprises four crystallographically independent subunits, while the other comprises two pairs of subunits related by a crystallographic twofold axis. The final model of 20 994 protein atoms, 1618 water molecules and 12 metal atoms refined to residuals R = 0.195 and R(free) = 0.215. The molecular structure confirms most of the previously reported features, including the subunit-subunit interfaces in the tetramer and persistent disorder at some residues. The metal-ligand bond lengths at the active site suggest that one of the two Mn atoms is five-coordinate rather than six-coordinate.
About this Structure
1M35 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution., Graham SC, Lee M, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):897-902. Epub 2003, Apr 25. PMID:12777807
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