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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2XG9 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]] 1.8Å</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=2xg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xg9 OCA], [https://pdbe.org/2xg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xg9 RCSB], [https://www.ebi.ac.uk/pdbsum/2xg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xg9 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xg9" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Amylase 3D structures|Amylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
[[Category: Denyer | [[Category: Large Structures]] | ||
[[Category: Field | [[Category: Denyer K]] | ||
[[Category: Lawson | [[Category: Field RA]] | ||
[[Category: Naldrett | [[Category: Lawson DM]] | ||
[[Category: Rejzek | [[Category: Naldrett MJ]] | ||
[[Category: Smith | [[Category: Rejzek M]] | ||
[[Category: Southard | [[Category: Smith AM]] | ||
[[Category: Stanley | [[Category: Southard AM]] | ||
[[Category: Stevenson | [[Category: Stanley D]] | ||
[[Category: Stevenson CEM]] | |||
Latest revision as of 08:47, 4 September 2024
Crystal structure of Barley Beta-Amylase complexed with 4-O-alpha-D- glucopyranosylmoranolineCrystal structure of Barley Beta-Amylase complexed with 4-O-alpha-D- glucopyranosylmoranoline
Structural highlights
FunctionPublication Abstract from PubMedThere 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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