2XGB

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

Summary for 2XGB

• Entry DOI: 10.2210/pdb2xgb/pdb
• Related: 1B1Y 2XFF 2XFR 2XFY 2XG9 2XGI
• Descriptor: BETA-AMYLASE, (2R)-oxiran-2-ylmethyl alpha-D-glucopyranoside, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: carbohydrate metabolism, hydrolase, germination
• Biological source: HORDEUM VULGARE (BARLEY)
• Total number of polymer chains: 1
• Total formula weight: 60154.59

Authors

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. (deposition date: 2010-06-02, release date: 2010-12-01, Last modification date: 2023-12-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.2 Å)