1apy: Difference between revisions
No edit summary |
No edit summary |
||
| Line 6: | Line 6: | ||
==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== | ||
| Line 22: | Line 25: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:01:02 2007'' | ||
Revision as of 16:54, 12 November 2007
|
HUMAN ASPARTYLGLUCOSAMINIDASE
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Aspartylglucosaminuria OMIM:[208400]
About this StructureAbout this Structure
1APY is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Active as N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 Structure known Active Sites: B1 and D1. Full crystallographic information is available from OCA.
ReferenceReference
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 Mon Nov 12 16:01:02 2007