2v3y
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2v3y |SIZE=350|CAPTION= <scene name='initialview01'>2v3y</scene>, resolution 1.60Å | |PDB= 2v3y |SIZE=350|CAPTION= <scene name='initialview01'>2v3y</scene>, resolution 1.60Å | ||
|SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+A'>AC3</scene> | |SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+A'>AC3</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1a16|1A16]], [[1jaw|1JAW]], [[1m35|1M35]], [[1n51|1N51]], [[1w2m|1W2M]], [[1w7v|1W7V]], [[1wbq|1WBQ]], [[1wl6|1WL6]], [[1wl9|1WL9]], [[1wlr|1WLR]], [[2bh3|2BH3]], [[2bha|2BHA]], [[2bhb|2BHB]], [[2bhc|2BHC]], [[2bhd|2BHD]], [[2bn7|2BN7]], [[2bws|2BWS]], [[2bwt|2BWT]], [[2bwu|2BWU]], [[2bwv|2BWV]], [[2bww|2BWW]], [[2bwx|2BWX]], [[2bwy|2BWY]], [[2v3x|2V3X]], [[2v3z|2V3Z]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3y OCA], [http://www.ebi.ac.uk/pdbsum/2v3y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v3y RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Graham, S C.]] | [[Category: Graham, S C.]] | ||
[[Category: Guss, J M.]] | [[Category: Guss, J M.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MN]] | ||
[[Category: pita-bread enzyme]] | [[Category: pita-bread enzyme]] | ||
[[Category: aminopeptidase]] | [[Category: aminopeptidase]] | ||
| Line 39: | Line 40: | ||
[[Category: protease]] | [[Category: protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:08:13 2008'' |
Revision as of 02:08, 31 March 2008
| |||||||
| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , | ||||||
| Activity: | Xaa-Pro aminopeptidase, with EC number 3.4.11.9 | ||||||
| Related: | 1A16, 1JAW, 1M35, 1N51, 1W2M, 1W7V, 1WBQ, 1WL6, 1WL9, 1WLR, 2BH3, 2BHA, 2BHB, 2BHC, 2BHD, 2BN7, 2BWS, 2BWT, 2BWU, 2BWV, 2BWW, 2BWX, 2BWY, 2V3X, 2V3Z
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT
Overview
Aminopeptidase P (APPro) is a manganese-containing enzyme that catalyses the hydrolysis of the N-terminal residue of a polypeptide if the second residue is proline. Structures of APPro mutants with reduced or negligible activity have been determined in complex with the tripeptide substrate ValProLeu. In the complex of Glu383Ala APPro with ValProLeu one of the two metal sites is only partly occupied, indicating an essential role for Glu383 in metal binding in the presence of substrate. His361Ala APPro clearly possesses residual activity as the ValProLeu substrate has been cleaved in the crystals; difference electron density consistent with bound ProLeu dipeptide and a disordered Val amino acid is present at the active site. Contrary to previous suggestions, the His243Ala mutant is capable of binding substrate. The structure of the His243Ala APPro complex with ValProLeu shows that the peptide interacts with one of the active-site metal atoms via its terminal amino group. The implications of these complexes for the roles of the respective residues in APPro catalysis are discussed.
About this Structure
2V3Y is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu., Graham SC, Guss JM, Arch Biochem Biophys. 2008 Jan 15;469(2):200-8. Epub 2007 Oct 24. PMID:17983589
Page seeded by OCA on Mon Mar 31 05:08:13 2008
