2o53: Difference between revisions

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[[Image:2o53.jpg|left|200px]]
[[Image:2o53.jpg|left|200px]]


{{Structure
<!--
|PDB= 2o53 |SIZE=350|CAPTION= <scene name='initialview01'>2o53</scene>, resolution 2.70&Aring;
The line below this paragraph, containing "STRUCTURE_2o53", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+314'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+B+314'>AC2</scene>, <scene name='pdbsite=AC3:Po4+Binding+Site+For+Residue+A+315'>AC3</scene>, <scene name='pdbsite=AC4:Po4+Binding+Site+For+Residue+A+316'>AC4</scene>, <scene name='pdbsite=AC5:Po4+Binding+Site+For+Residue+B+315'>AC5</scene> and <scene name='pdbsite=AC6:Po4+Binding+Site+For+Residue+B+316'>AC6</scene>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartoacylase Aspartoacylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.15 3.5.1.15] </span>
or leave the SCENE parameter empty for the default display.
|GENE= ASPA, ACY2, ASP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
-->
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK02259 PRK02259]</span>
{{STRUCTURE_2o53| PDB=2o53  | SCENE= }}  
|RELATEDENTRY=[[2o4h|2O4H]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o53 OCA], [http://www.ebi.ac.uk/pdbsum/2o53 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o53 RCSB]</span>
}}


'''Crystal structure of apo-Aspartoacylase from human brain'''
'''Crystal structure of apo-Aspartoacylase from human brain'''
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[[Category: Sanishvili, R.]]
[[Category: Sanishvili, R.]]
[[Category: Viola, R E.]]
[[Category: Viola, R E.]]
[[Category: acy2]]
[[Category: Acy2]]
[[Category: aminoacylase-2]]
[[Category: Aminoacylase-2]]
[[Category: aspa]]
[[Category: Aspa]]
[[Category: aspartoacylase family]]
[[Category: Aspartoacylase family]]
[[Category: canavan disease]]
[[Category: Canavan disease]]
[[Category: n-acetyl-l-aspartate]]
[[Category: N-acetyl-l-aspartate]]
[[Category: n-phosphonomethyl-l-aspartate]]
[[Category: N-phosphonomethyl-l-aspartate]]
[[Category: zinc-dependent hydrolase]]
[[Category: Zinc-dependent hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:20:09 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 2 11:31:40 2008''

Revision as of 10:20, 4 May 2008

File:2o53.jpg

Template:STRUCTURE 2o53

Crystal structure of apo-Aspartoacylase from human brain


OverviewOverview

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.

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 Page seeded by OCA on Sun May 4 10:20:09 2008

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