View source for 2xgb


==Crystal structure of Barley Beta-Amylase complexed with 2,3- epoxypropyl-alpha-D-glucopyranoside==
<StructureSection load='2xgb' size='340' side='right'caption='[[2xgb]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xgb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPG:2-HYDROXYMETHYL-6-OXIRANYLMETHOXY-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>EPG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgb OCA], [https://pdbe.org/2xgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgb RCSB], [https://www.ebi.ac.uk/pdbsum/2xgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMYB_HORVU AMYB_HORVU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 beta-amylase of the grain endosperm (BMY1). The molecular basis of inhibitor action was defined through high resolution X-ray crystallography studies of unliganded barley beta-amylase, as well as its complexes with glycone site binder disaccharide iminosugar G1M, irreversible inhibitors alpha-epoxypropyl and alpha-epoxybutyl glucosides, which target the enzyme's catalytic residues, and the aglycone site binders acarbose and alpha-cyclodextrin.

Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley beta-amylase.,Rejzek M, Stevenson CE, Southard AM, Stanley D, Denyer K, Smith AM, Naldrett MJ, Lawson DM, Field RA Mol Biosyst. 2010 Nov 18. PMID:21085740<ref>PMID:21085740</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2xgb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Amylase 3D structures|Amylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hordeum vulgare]]
[[Category: Large Structures]]
[[Category: Denyer K]]
[[Category: Field RA]]
[[Category: Lawson DM]]
[[Category: Naldrett MJ]]
[[Category: Rejzek M]]
[[Category: Smith AM]]
[[Category: Southard AM]]
[[Category: Stanley D]]
[[Category: Stevenson CEM]]