1APZ

HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT

1APZ の概要

• エントリーDOI: 10.2210/pdb1apz/pdb
• 分子名称: 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)
• 機能のキーワード: aspartylglucosaminidase, glycosylasparaginase, complex (hydrolase-peptide), complex (hydrolase-peptide) complex, complex (hydrolase/peptide)
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Lysosome: P20933 P20933
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66273.28

構造登録者

Rouvinen, J.,Oinonen, C. (登録日: 1995-06-14, 公開日: 1996-12-23, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)