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.


2imo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2imo.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2imo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2imo| PDB=2imo | SCENE= }}
{{STRUCTURE_2imo| PDB=2imo | SCENE= }}
-
'''Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6'''
+
===Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6===
-
==Overview==
+
<!--
-
Purine metabolism plays a major role in regulating the availability of purine nucleotides destined for nucleic acid synthesis. Allantoate amidohydrolase catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. The crystal structure of a ternary complex of allantoate amidohydrolase with its substrate allantoate and an allosteric effector, a sulfate ion, from Escherichia coli was determined to understand better the catalytic mechanism and substrate specificity. The 2.25 A resolution X-ray structure reveals an alpha/beta scaffold akin to zinc exopeptidases of the peptidase M20 family and lacks the (beta/alpha)(8)-barrel fold characteristic of the amidohydrolases. Arrangement of the substrate and the two co-catalytic zinc ions at the active site governs catalytic specificity for hydrolysis of N-carbamyl versus the peptide bond in exopeptidases. In its crystalline form, allantoate amidohydrolase adopts a relatively open conformation. However, structural analysis reveals the possibility of a significant movement of domains via rotation about two hinge regions upon allosteric effector and substrate binding resulting in a closed catalytically competent conformation by bringing the substrate allantoate closer to co-catalytic zinc ions. Two cis-prolyl peptide bonds found on either side of the dimerization domain in close proximity to the substrate and ligand-binding sites may be involved in protein folding and in preserving the integrity of the catalytic site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17362992}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17362992 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17362992}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: T1507]]
[[Category: T1507]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:39:52 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:57:20 2008''

Revision as of 16:57, 28 July 2008

Image:2imo.png

Template:STRUCTURE 2imo

Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6

Template:ABSTRACT PUBMED 17362992

About this Structure

2IMO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics., Agarwal R, Burley SK, Swaminathan S, J Mol Biol. 2007 Apr 27;368(2):450-63. Epub 2007 Feb 20. PMID:17362992

Page seeded by OCA on Mon Jul 28 19:57:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2imo"
Personal tools