1apz
From Proteopedia
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|PDB= 1apz |SIZE=350|CAPTION= <scene name='initialview01'>1apz</scene>, resolution 2.3Å | |PDB= 1apz |SIZE=350|CAPTION= <scene name='initialview01'>1apz</scene>, resolution 2.3Å | ||
|SITE= <scene name='pdbsite=B:A+Catalytic+Residue'>B</scene> and <scene name='pdbsite=D:A+Catalytic+Residue'>D</scene> | |SITE= <scene name='pdbsite=B:A+Catalytic+Residue'>B</scene> and <scene name='pdbsite=D:A+Catalytic+Residue'>D</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1apz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apz OCA], [http://www.ebi.ac.uk/pdbsum/1apz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1apz RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Aspartylglucosaminuria OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=208400 208400]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Oinonen, C.]] | [[Category: Oinonen, C.]] | ||
[[Category: Rouvinen, J.]] | [[Category: Rouvinen, J.]] | ||
| - | [[Category: ASP]] | ||
| - | [[Category: NAG]] | ||
[[Category: aspartylglucosaminidase]] | [[Category: aspartylglucosaminidase]] | ||
[[Category: complex (hydrolase/peptide)]] | [[Category: complex (hydrolase/peptide)]] | ||
[[Category: glycosylasparaginase]] | [[Category: glycosylasparaginase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:15 2008'' |
Revision as of 15:45, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , | ||||||
| Activity: | N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT
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
1APZ 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 Sun Mar 30 18:45:15 2008
