Journal article

Publication year: 1995

Pages: 1102-1108

Journal: Nature Structural Biology

Volume number: 2

Issue number: 12

ISSN: 1072-8368

DOI Link: https://doi.org/10.1038/nsb1295-1102

Publisher: Nature America

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 (ACU), a lysosomal storage disease.

Harvard Citation style: Oinonen, C., Tikkanen, R., Rouvinen, J. and Peltonen, L. (1995) Three-dimensional structure of human lysosomal aspartylglucosaminidase, Nature Structural Biology, 2(12), pp. 1102-1108. https://doi.org/10.1038/nsb1295-1102

APA Citation style: Oinonen, C., Tikkanen, R., Rouvinen, J., & Peltonen, L. (1995). Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nature Structural Biology. 2(12), 1102-1108. https://doi.org/10.1038/nsb1295-1102