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Three-dimensional structure of human lysosomal aspartylglucosaminidase.

Authors
Type
Published Article
Journal
Natural Structural Biology
1072-8368
Publisher
Nature Publishing Group
Publication Date
Volume
2
Issue
12
Pages
1102–1108
Identifiers
PMID: 8846222
Source
Medline

Abstract

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.

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