5DL0

Crystal structure of glucosidase II alpha subunit (Glc1Man2-bound from)

5DL0 の概要

• エントリーDOI: 10.2210/pdb5dl0/pdb
• 関連するPDBエントリー: 5DKX 5DKY 5DKZ
• 分子名称: Alpha glucosidase-like protein, alpha-D-glucopyranose-(1-3)-alpha-D-mannopyranose (3 entities in total)
• 機能のキーワード: endoplasmic reticulum, glycoside hydrolase, glycosylation, hydrolase
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 108799.45

構造登録者

Satoh, T.,Toshimori, T.,Yan, G.,Yamaguchi, T.,Kato, K. (登録日: 2015-09-04, 公開日: 2016-01-27, 最終更新日: 2024-10-30)

主引用文献

Satoh, T.,Toshimori, T.,Yan, G.,Yamaguchi, T.,Kato, K.
Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control.
Sci Rep, 6:20575-20575, 2016

PubMed Abstract: The endoplasmic reticulum (ER) has a sophisticated protein quality control system for the efficient folding of newly synthesized proteins. In this system, a variety of N-linked oligosaccharides displayed on proteins serve as signals recognized by series of intracellular lectins. Glucosidase II catalyzes two-step hydrolysis at α1,3-linked glucose-glucose and glucose-mannose residues of high-mannose-type glycans to generate a quality control protein tag that is transiently expressed on glycoproteins and recognized by ER chaperones. Here we determined the crystal structures of the catalytic α subunit of glucosidase II (GIIα) complexed with two different glucosyl ligands containing the scissile bonds of first- and second-step reactions. Our structural data revealed that the nonreducing terminal disaccharide moieties of the two kinds of substrates can be accommodated in a gourd-shaped bilocular pocket, thereby providing a structural basis for substrate-binding specificity in the two-step deglucosylation catalyzed by this enzyme.

PubMed: 26847925
DOI: 10.1038/srep20575

実験手法

X-RAY DIFFRACTION (2.3 Å)