1ve6: Difference between revisions
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[[Image:1ve6.gif|left|200px]] | [[Image:1ve6.gif|left|200px]] | ||
'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1''' | {{Structure | ||
|PDB= 1ve6 |SIZE=350|CAPTION= <scene name='initialview01'>1ve6</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] | |||
|GENE= | |||
}} | |||
'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1VE6 is a [ | 1VE6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VE6 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1., Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z, Structure. 2004 Aug;12(8):1481-8. PMID:[http:// | Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1., Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z, Structure. 2004 Aug;12(8):1481-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15296741 15296741] | ||
[[Category: Acylaminoacyl-peptidase]] | [[Category: Acylaminoacyl-peptidase]] | ||
[[Category: Aeropyrum pernix]] | [[Category: Aeropyrum pernix]] | ||
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[[Category: beta propeller domain]] | [[Category: beta propeller domain]] | ||
''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 14:44:19 2008'' | ||
Revision as of 15:44, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Acylaminoacyl-peptidase, with EC number 3.4.19.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1
OverviewOverview
Acylpeptide hydrolases (APH; also known as acylamino acid releasing enzyme) catalyze the removal of an N-acylated amino acid from blocked peptides. The crystal structure of an APH from the thermophilic archaeon Aeropyrum pernix K1 to 2.1 A resolution confirms it to be a member of the prolyl oligopeptidase family of serine proteases. The structure of apAPH is a symmetric homodimer with each subunit comprised of two domains. The N-terminal domain is a regular seven-bladed beta-propeller, while the C-terminal domain has a canonical alpha/beta hydrolase fold and includes the active site and a conserved Ser445-Asp524-His556 catalytic triad. The complex structure of apAPH with an organophosphorus substrate, p-nitrophenyl phosphate, has also been determined. The complex structure unambiguously maps out the substrate binding pocket and provides a basis for substrate recognition by apAPH. A conserved mechanism for protein degradation from archaea to mammals is suggested by the structural features of apAPH.
About this StructureAbout this Structure
1VE6 is a Single protein structure of sequence from Aeropyrum pernix. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1., Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z, Structure. 2004 Aug;12(8):1481-8. PMID:15296741
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