1ve6

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(New page: 200px<br /><applet load="1ve6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ve6, resolution 2.1&Aring;" /> '''Crystal structure of ...)
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caption="1ve6, resolution 2.1&Aring;" />
'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1'''<br />
'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1VE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with BOG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VE6 OCA].
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1VE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with <scene name='pdbligand=BOG:'>BOG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VE6 OCA].
==Reference==
==Reference==
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[[Category: beta propeller domain]]
[[Category: beta propeller domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:46:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:18 2008''

Revision as of 13:34, 21 February 2008


1ve6, resolution 2.1Å

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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 with and as ligands. Active as Acylaminoacyl-peptidase, with EC number 3.4.19.1 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

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