2o53: Difference between revisions

Revision as of 06:31, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2o53.png

Template:STRUCTURE 2o53

Crystal structure of apo-Aspartoacylase from human brainCrystal structure of apo-Aspartoacylase from human brain

Template:ABSTRACT PUBMED 18293939

About this StructureAbout this Structure

2O53 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Examination of the Mechanism of Human Brain Aspartoacylase through the Binding of an Intermediate Analogue(,)., Le Coq J, Pavlovsky A, Malik R, Sanishvili R, Xu C, Viola RE, Biochemistry. 2008 Mar 18;47(11):3484-92. Epub 2008 Feb 23. PMID:18293939

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of apo-Aspartoacylase from human brain'''
+===Crystal structure of apo-Aspartoacylase from human brain===
-==Overview==
+<!--
-Canavan disease is a fatal neurological disorder caused by the malfunctioning of a single metabolic enzyme, aspartoacylase, that catalyzes the deacetylation of N-acetyl- l-aspartate to produce l-aspartate and acetate. The structure of human brain aspartoacylase has been determined in complex with a stable tetrahedral intermediate analogue, N-phosphonomethyl- l-aspartate. This potent inhibitor forms multiple interactions between each of its heteroatoms and the substrate binding groups arrayed within the active site. The binding of the catalytic intermediate analogue induces the conformational ordering of several substrate binding groups, thereby setting up the active site for catalysis. The highly ordered binding of this inhibitor has allowed assignments to be made for substrate binding groups and provides strong support for a carboxypeptidase-type mechanism for the hydrolysis of the amide bond of the substrate, N-acetyl- l-aspartate.
+The line below this paragraph, {{ABSTRACT_PUBMED_18293939}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18293939 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18293939}}
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 [[Category: N-phosphonomethyl-l-aspartate]]
 [[Category: Zinc-dependent hydrolase]]
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