1APZ

HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT

Summary for 1APZ

• Entry DOI: 10.2210/pdb1apz/pdb
• Descriptor: ASPARTYLGLUCOSAMINIDASE, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: aspartylglucosaminidase, glycosylasparaginase, complex (hydrolase-peptide), complex (hydrolase-peptide) complex, complex (hydrolase/peptide)
• Biological source: Homo sapiens (human); More
• Cellular location: Lysosome: P20933 P20933
• Total number of polymer chains: 4
• Total formula weight: 66273.28

Authors

Rouvinen, J.,Oinonen, C. (deposition date: 1995-06-14, release date: 1996-12-23, Last modification date: 2024-10-23)

Primary citation

Oinonen, C.,Tikkanen, R.,Rouvinen, J.,Peltonen, L.
Three-dimensional structure of human lysosomal aspartylglucosaminidase.
Nat.Struct.Biol., 2:1102-1108, 1995

PubMed 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.

PubMed: 8846222
DOI: 10.1038/nsb1295-1102

Experimental method

X-RAY DIFFRACTION (2.3 Å)