1PS3

Golgi alpha-mannosidase II in complex with kifunensine

1PS3 の概要

• エントリーDOI: 10.2210/pdb1ps3/pdb
• 関連するPDBエントリー: 1HTY 1HWW 1HXK
• 分子名称: Alpha-mannosidase II, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total)
• 機能のキーワード: glycosyl hydrolase, mannosidase, n-terminal alpha-beta domain, three helix bundle, 2 c-terminal beta barrels, 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: 120230.63

構造登録者

Shah, N.,Kuntz, D.A.,Rose, D.R. (登録日: 2003-06-20, 公開日: 2003-12-16, 最終更新日: 2024-10-16)

主引用文献

Shah, N.,Kuntz, D.A.,Rose, D.R.
Comparison of Kifunensine and 1-Deoxymannojirimycin Binding to Class I and II alpha-Mannosidases Demonstrates Different Saccharide Distortions in Inverting and Retaining Catalytic Mechanisms
Biochemistry, 42:13812-13816, 2003

PubMed Abstract: Mannosidases are key enzymes in the eukaryotic N-glycosylation pathway. These enzymes fall into two broad classes (I and II) and are characteristically different in catalytic mechanism, sequence, and structure. Kifunensine is an alkaloid that is a strong inhibitor against class I alpha-mannosidases but is only a weak inhibitor against class II alpha-mannosidases. In this paper, the 1.80 A resolution crystal structure of kifunensine bound to Drosophila melanogaster Golgi alpha-mannosidase II (dGMII) is presented. Kifunensine adopts a (1,4)B boat conformation in the class II dGMII, which contrasts the (1)C(4) chair conformation seen in class I human endoplasmic reticulum alpha1,2 mannosidase (hERMI, PDB ). The observed conformations are higher in conformational energy than the global minimum (4)C(1) conformation, although the conformation in hERMI is closer to the minimum, as supported by an energy calculation. Differing conformations of 1-deoxymannojirimycin were also observed: a (4)C(1) and (1)C(4) conformation in dGMII and hERMI, respectively. Thus, these two alpha-mannosidase classes distort these inhibitors in distinct manners. This is likely indicative of the binding characteristics of the two different catalytic mechanisms of these enzymes.

PubMed: 14636047
DOI: 10.1021/bi034742r

実験手法

X-RAY DIFFRACTION (1.8 Å)