3THC

Crystal structure of human beta-galactosidase in complex with galactose

3THC の概要

• エントリーDOI: 10.2210/pdb3thc/pdb
• 関連するPDBエントリー: 3LHD
• 分子名称: Beta-galactosidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: beta-galactosidase, tim-barrel domain, glycosyl hydrolase, glycosylation, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Lysosome. Isoform 2: Cytoplasm, perinuclear region: P16278
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 300328.16

構造登録者

Ohto, U.,Shimizu, T. (登録日: 2011-08-18, 公開日: 2011-12-07, 最終更新日: 2024-10-16)

主引用文献

Ohto, U.,Usui, K.,Ochi, T.,Yuki, K.,Satow, Y.,Shimizu, T.
Crystal structure of human beta-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases
J.Biol.Chem., 287:1801-1812, 2012

PubMed Abstract: G(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed.

PubMed: 22128166
DOI: 10.1074/jbc.M111.293795

実験手法

X-RAY DIFFRACTION (1.8 Å)