1apy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1apy.gif|left|200px]]
[[Image:1apy.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1apy |SIZE=350|CAPTION= <scene name='initialview01'>1apy</scene>, resolution 2.0&Aring;
+
The line below this paragraph, containing "STRUCTURE_1apy", creates the "Structure Box" on the page.
-
|SITE= <scene name='pdbsite=B1:A+Catalytic+Residue'>B1</scene> and <scene name='pdbsite=D1:A+Catalytic+Residue'>D1</scene>
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1apy| PDB=1apy | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [http://www.ebi.ac.uk/pdbsum/1apy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB]</span>
+
-
}}
+
'''HUMAN ASPARTYLGLUCOSAMINIDASE'''
'''HUMAN ASPARTYLGLUCOSAMINIDASE'''
Line 24: Line 21:
Three-dimensional structure of human lysosomal aspartylglucosaminidase., Oinonen C, Tikkanen R, Rouvinen J, Peltonen L, Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8846222 8846222]
Three-dimensional structure of human lysosomal aspartylglucosaminidase., Oinonen C, Tikkanen R, Rouvinen J, Peltonen L, Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8846222 8846222]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Oinonen, C.]]
[[Category: Oinonen, C.]]
[[Category: Rouvinen, J.]]
[[Category: Rouvinen, J.]]
-
[[Category: aspartylglucosaminidase]]
+
[[Category: Aspartylglucosaminidase]]
-
[[Category: glycosylasparaginase]]
+
[[Category: Glycosylasparaginase]]
-
[[Category: hydrolase]]
+
[[Category: Hydrolase]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:34:01 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:12 2008''
+

Revision as of 07:34, 2 May 2008

Template:STRUCTURE 1apy

HUMAN ASPARTYLGLUCOSAMINIDASE


Overview

The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined. This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits. Two alpha- and beta-chains are found to pack together forming the final heterotetrameric structure. The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site. On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum. The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.

About this Structure

1APY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of human lysosomal aspartylglucosaminidase., Oinonen C, Tikkanen R, Rouvinen J, Peltonen L, Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222 Page seeded by OCA on Fri May 2 10:34:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools