2XGI

Crystal structure of Barley Beta-Amylase complexed with 3,4- epoxybutyl alpha-D-glucopyranoside

2XGI の概要

• エントリーDOI: 10.2210/pdb2xgi/pdb
• 関連するPDBエントリー: 1B1Y 2XFF 2XFR 2XFY 2XG9 2XGB
• 分子名称: BETA-AMYLASE, 1,2-ETHANEDIOL, (3R)-3-hydroxybutyl alpha-D-glucopyranoside, ... (5 entities in total)
• 機能のキーワード: glycosidase, carbohydrate metabolism, glycosyl hydrolase family 14, starch degradation, germination, hydrolase
• 由来する生物種: HORDEUM VULGARE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60298.76

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: 2010-06-04, 公開日: 2010-12-01, 最終更新日: 2024-11-13)

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, 7:718-730, 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 (1.3 Å)