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.


1or0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1or0.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1or0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1or0| PDB=1or0 | SCENE= }}
{{STRUCTURE_1or0| PDB=1or0 | SCENE= }}
-
'''Crystal Structures of Glutaryl 7-Aminocephalosporanic Acid Acylase: Insight into Autoproteolytic Activation'''
+
===Crystal Structures of Glutaryl 7-Aminocephalosporanic Acid Acylase: Insight into Autoproteolytic Activation===
-
==Overview==
+
<!--
-
Glutaryl 7-aminocephalosporanic acid acylase (GCA, EC 3.5.1.11) is a member of N-terminal nucleophile (Ntn) hydrolases. The native enzyme is an (alpha beta)(2) heterotetramer originated from an enzymatically inactive precursor of a single polypeptide. The activation of precursor GCA consists of primary and secondary autoproteolytic cleavages, generating a terminal residue with both a nucleophile and a base and releasing a nine amino acid spacer peptide. We have determined the crystal structures of the recombinant selenomethionyl native and S170A mutant precursor from Pseudomonas sp. strain GK16. Precursor activation is likely triggered by conformational constraints within the spacer peptide, probably inducing a peptide flip. Autoproteolytic site solvent molecules, which have been trapped in a hydrophobic environment by the spacer peptide, may play a role as a general base for nucleophilic attack. The activation results in building up a catalytic triad composed of Ser170/His192/Glu624. However, the triad is not linked to the usual hydroxyl but the free alpha-amino group of the N-terminal serine residue of the native GCA. Mutagenesis and structural data support the notion that the stabilization of a transient hydroxazolidine ring during autoproteolysis would be critical during the N --&gt; O acyl shift. The autoproteolytic activation mechanism for GCA is described.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12680762}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12680762 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12680762}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Glutaryl 7-aminocephalosporanic acid]]
[[Category: Glutaryl 7-aminocephalosporanic acid]]
[[Category: Glutaryl 7-aminocephalosporanic acid acylase]]
[[Category: Glutaryl 7-aminocephalosporanic acid acylase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:10:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:10:42 2008''

Revision as of 13:10, 27 July 2008

Image:1or0.png

Template:STRUCTURE 1or0

Crystal Structures of Glutaryl 7-Aminocephalosporanic Acid Acylase: Insight into Autoproteolytic Activation

Template:ABSTRACT PUBMED 12680762

About this Structure

1OR0 is a Protein complex structure of sequences from Pseudomonas sp. sy-77. Full crystallographic information is available from OCA.

Reference

Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation., Kim JK, Yang IS, Rhee S, Dauter Z, Lee YS, Park SS, Kim KH, Biochemistry. 2003 Apr 15;42(14):4084-93. PMID:12680762

Page seeded by OCA on Sun Jul 27 16:10:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1or0"
Personal tools