2XGB

Crystal structure of Barley Beta-Amylase complexed with 2,3- epoxypropyl-alpha-D-glucopyranoside

2XGB の概要

• エントリーDOI: 10.2210/pdb2xgb/pdb
• 関連するPDBエントリー: 1B1Y 2XFF 2XFR 2XFY 2XG9 2XGI
• 分子名称: BETA-AMYLASE, (2R)-oxiran-2-ylmethyl alpha-D-glucopyranoside, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: carbohydrate metabolism, hydrolase, germination
• 由来する生物種: HORDEUM VULGARE (BARLEY)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60154.59

構造登録者

Rejzek, M.,Stevenson, C.E.M.,Southard, A.M.,Stanley, D.,Denyer, K.,Smith, A.M.,Naldrett, M.J.,Lawson, D.M.,Field, R.A. (登録日: 2010-06-02, 公開日: 2010-12-01, 最終更新日: 2023-12-20)

主引用文献

Rejzek, M.,Stevenson, C.E.,Southard, A.M.,Stanley, D.,Denyer, K.,Smith, A.M.,Naldrett, M.J.,Lawson, D.M.,Field, R.A.
Chemical Genetics and Cereal Starch Metabolism: Structural Basis of the Non-Covalent and Covalent Inhibition of Barley Beta-Amylase.
Mol.Biosyst., 7:718-, 2011

PubMed Abstract: There are major issues regarding the proposed pathway for starch degradation in germinating cereal grain. Given the commercial importance but genetic intractability of the problem, we have embarked on a program of chemical genetics studies to identify and dissect the pathway and regulation of starch degradation in germinating barley grains. As a precursor to in vivo studies, here we report systematic analysis of the reversible and irreversible inhibition of the major β-amylase of the grain endosperm (BMY1). The molecular basis of inhibitor action was defined through high resolution X-ray crystallography studies of unliganded barley β-amylase, as well as its complexes with glycone site binder disaccharide iminosugar G1M, irreversible inhibitors α-epoxypropyl and α-epoxybutyl glucosides, which target the enzyme's catalytic residues, and the aglycone site binders acarbose and α-cyclodextrin.

PubMed: 21085740
DOI: 10.1039/C0MB00204F

実験手法

X-RAY DIFFRACTION (1.2 Å)