1QWN

GOLGI ALPHA-MANNOSIDASE II Covalent Intermediate Complex with 5-fluoro-gulosyl-fluoride

1QWN の概要

• エントリーDOI: 10.2210/pdb1qwn/pdb
• 関連するPDBエントリー: 1HTY 1HWW 1HXK 1PS3 1QWU 1QX1
• 分子名称: Alpha-mannosidase II, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (7 entities in total)
• 機能のキーワード: n-terminal alpha-beta domain, three helix bundle, 2 c-terminal beta barrels, family 38 glycosyl hydrolase, hydrolase
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 120428.69

構造登録者

Numao, S.,Kuntz, D.A.,Withers, S.G.,Rose, D.R. (登録日: 2003-09-02, 公開日: 2003-10-07, 最終更新日: 2024-11-06)

主引用文献

Numao, S.,Kuntz, D.A.,Withers, S.G.,Rose, D.R.
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates.
J.Biol.Chem., 278:48074-48083, 2003

PubMed Abstract: The family 38 golgi alpha-mannosidase II, thought to cleave mannosidic bonds through a double displacement mechanism involving a reaction intermediate, is a clinically important enzyme involved in glycoprotein processing. The structure of three different covalent glycosyl-enzyme intermediates have been determined to 1.2-A resolution for the Golgi alpha-mannosidase II from Drosophila melanogaster by use of fluorinated sugar analogues, both with the wild-type enzyme and a mutant enzyme in which the acid/base catalyst has been removed. All these structures reveal sugar intermediates bound in a distorted 1S5 skew boat conformation. The similarity of this conformation with that of the substrate in the recently determined structure of the Michaelis complex of a beta-mannanase (Ducros, V. M. A., Zechel, D. L., Murshudov, G. N., Gilbert, H. J., Szabo, L., Stoll, D., Withers, S. G., and Davies, G. J. (2002) Angew. Chem. Int. Ed. Engl. 41, 2824-2827) suggests that these disparate enzymes have recruited common stereoelectronic features in evolving their catalytic mechanisms.

PubMed: 12960159
DOI: 10.1074/jbc.M309249200

実験手法

X-RAY DIFFRACTION (1.2 Å)