1ve6

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[[Image:1ve6.gif|left|200px]]
[[Image:1ve6.gif|left|200px]]
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{{Structure
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|PDB= 1ve6 |SIZE=350|CAPTION= <scene name='initialview01'>1ve6</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1ve6", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1ve6| PDB=1ve6 | SCENE= }}
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|RELATEDENTRY=[[1ve7|1VE7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ve6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve6 OCA], [http://www.ebi.ac.uk/pdbsum/1ve6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ve6 RCSB]</span>
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'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1'''
'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1'''
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[[Category: Yang, H.]]
[[Category: Yang, H.]]
[[Category: Zhao, X.]]
[[Category: Zhao, X.]]
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[[Category: alpha/beta hydrolase domain]]
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[[Category: Alpha/beta hydrolase domain]]
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[[Category: beta propeller domain]]
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[[Category: Beta propeller domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:26:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:23:07 2008''
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Revision as of 09:26, 3 May 2008

Image:1ve6.gif

Template:STRUCTURE 1ve6

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1


Overview

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 Structure

1VE6 is a Single protein structure of sequence from Aeropyrum pernix. Full crystallographic information is available from OCA.

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:15296741 Page seeded by OCA on Sat May 3 12:26:05 2008

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