This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ve6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ve6.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ve6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ve6| PDB=1ve6 | SCENE= }}
{{STRUCTURE_1ve6| PDB=1ve6 | SCENE= }}
-
'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15296741}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15296741 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15296741}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Alpha/beta hydrolase domain]]
[[Category: Alpha/beta hydrolase domain]]
[[Category: Beta propeller domain]]
[[Category: Beta propeller domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:26:05 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:33:26 2008''

Revision as of 21:33, 28 July 2008

Image:1ve6.png

Template:STRUCTURE 1ve6

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

Template:ABSTRACT PUBMED 15296741

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 Tue Jul 29 00:33:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ve6"
Personal tools