2i3c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2i3c.gif|left|200px]]
[[Image:2i3c.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2i3c |SIZE=350|CAPTION= <scene name='initialview01'>2i3c</scene>, resolution 2.800&Aring;
+
The line below this paragraph, containing "STRUCTURE_2i3c", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <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_2i3c| PDB=2i3c | SCENE= }}
-
|RELATEDENTRY=[[2gu2|2gu2]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3c OCA], [http://www.ebi.ac.uk/pdbsum/2i3c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i3c RCSB]</span>
+
-
}}
+
'''Crystal Structure of an Aspartoacylase from Homo Sapiens'''
'''Crystal Structure of an Aspartoacylase from Homo Sapiens'''
Line 32: Line 29:
[[Category: Mccoy, J G.]]
[[Category: Mccoy, J G.]]
[[Category: Wesenberg, G E.]]
[[Category: Wesenberg, G 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: center for eukaryotic structural genomic]]
+
[[Category: Center for eukaryotic structural genomic]]
-
[[Category: cesg]]
+
[[Category: Cesg]]
-
[[Category: n-acetyl-l-aspartate]]
+
[[Category: N-acetyl-l-aspartate]]
-
[[Category: protein structure initiative]]
+
[[Category: Protein structure initiative]]
-
[[Category: psi]]
+
[[Category: Psi]]
-
[[Category: zinc-dependent hydrolase]]
+
[[Category: Zinc-dependent hydrolase]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:01:13 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:39:07 2008''
+

Revision as of 04:01, 4 May 2008

Image:2i3c.gif

Template:STRUCTURE 2i3c

Crystal Structure of an Aspartoacylase from Homo Sapiens


Overview

Aspartoacylase catalyzes hydrolysis of N-acetyl-l-aspartate to aspartate and acetate in the vertebrate brain. Deficiency in this activity leads to spongiform degeneration of the white matter of the brain and is the established cause of Canavan disease, a fatal progressive leukodystrophy affecting young children. We present crystal structures of recombinant human and rat aspartoacylase refined to 2.8- and 1.8-A resolution, respectively. The structures revealed that the N-terminal domain of aspartoacylase adopts a protein fold similar to that of zinc-dependent hydrolases related to carboxypeptidases A. The catalytic site of aspartoacylase shows close structural similarity to those of carboxypeptidases despite only 10-13% sequence identity between these proteins. About 100 C-terminal residues of aspartoacylase form a globular domain with a two-stranded beta-sheet linker that wraps around the N-terminal domain. The long channel leading to the active site is formed by the interface of the N- and C-terminal domains. The C-terminal domain is positioned in a way that prevents productive binding of polypeptides in the active site. The structures revealed that residues 158-164 may undergo a conformational change that results in opening and partial closing of the channel entrance. We hypothesize that the catalytic mechanism of aspartoacylase is closely analogous to that of carboxypeptidases. We identify residues involved in zinc coordination, and propose which residues may be involved in substrate binding and catalysis. The structures also provide a structural framework necessary for understanding the deleterious effects of many missense mutations of human aspartoacylase.

About this Structure

2I3C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of aspartoacylase, the brain enzyme impaired in Canavan disease., Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN Jr, Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):456-61. Epub 2006 Dec 28. PMID:17194761 Page seeded by OCA on Sun May 4 07:01:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i3c"
Personal tools