2xg9: Difference between revisions
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[[ | ==Crystal structure of Barley Beta-Amylase complexed with 4-O-alpha-D- glucopyranosylmoranoline== | ||
<StructureSection load='2xg9' size='340' side='right' caption='[[2xg9]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xg9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XG9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XG9 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xfy|2xfy]], [[2xff|2xff]], [[1b1y|1b1y]], [[2xfr|2xfr]], [[2xgb|2xgb]], [[2xgi|2xgi]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xg9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xg9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xg9 PDBsum]</span></td></tr> | |||
<table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[Amylase|Amylase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Beta-amylase]] | [[Category: Beta-amylase]] | ||
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] |