2XGI
Crystal structure of Barley Beta-Amylase complexed with 3,4- epoxybutyl alpha-D-glucopyranoside
Summary for 2XGI
| Entry DOI | 10.2210/pdb2xgi/pdb |
| Related | 1B1Y 2XFF 2XFR 2XFY 2XG9 2XGB |
| Descriptor | BETA-AMYLASE, 1,2-ETHANEDIOL, (3R)-3-hydroxybutyl alpha-D-glucopyranoside, ... (5 entities in total) |
| Functional Keywords | glycosidase, carbohydrate metabolism, glycosyl hydrolase family 14, starch degradation, germination, hydrolase |
| Biological source | HORDEUM VULGARE |
| Total number of polymer chains | 1 |
| Total formula weight | 60298.76 |
| 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: 2010-06-04, release date: 2010-12-01, Last modification date: 2024-11-13) |
| 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, 7:718-730, 2011 Cited by 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: 21085740DOI: 10.1039/c0mb00204f PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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