1DL2

CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION

1DL2 の概要

• エントリーDOI: 10.2210/pdb1dl2/pdb
• 分子名称: CLASS I ALPHA-1,2-MANNOSIDASE, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: alpha-alpha helix barrel, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60948.04

構造登録者

Vallee, F.,Lipari, F.,Yip, P.,Herscovics, A.,Howell, P.L. (登録日: 1999-12-08, 公開日: 2000-02-18, 最終更新日: 2024-11-13)

主引用文献

Vallee, F.,Lipari, F.,Yip, P.,Sleno, B.,Herscovics, A.,Howell, P.L.
Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control.
EMBO J., 19:581-588, 2000

PubMed Abstract: Mannose trimming is not only essential for N-glycan maturation in mammalian cells but also triggers degradation of misfolded glycoproteins. The crystal structure of the class I alpha1, 2-mannosidase that trims Man(9)GlcNAc(2) to Man(8)GlcNAc(2 )isomer B in the endoplasmic reticulum of Saccharomyces cerevisiae reveals a novel (alphaalpha)(7)-barrel in which an N-glycan from one molecule extends into the barrel of an adjacent molecule, interacting with the essential acidic residues and calcium ion. The observed protein-carbohydrate interactions provide the first insight into the catalytic mechanism and specificity of this eukaryotic enzyme family and may be used to design inhibitors that prevent degradation of misfolded glycoproteins in genetic diseases.

PubMed: 10675327
DOI: 10.1093/emboj/19.4.581

実験手法

X-RAY DIFFRACTION (1.54 Å)