View source for 6gya


==Amylase in complex with branched ligand==
<StructureSection load='6gya' size='340' side='right'caption='[[6gya]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gya]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_sp. Alicyclobacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GYA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GYA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gya OCA], [http://pdbe.org/6gya PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gya RCSB], [http://www.ebi.ac.uk/pdbsum/6gya PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gya ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
alpha-Amylases are glycoside hydrolases that break the alpha-1,4 bonds in starch and related glycans. The degradation of starch is rendered difficult by the presence of varying degrees of alpha-1,6 branch points and their possible accommodation within the active centre of alpha-amylase enzymes. Given the myriad industrial uses for starch and thus also for alpha-amylase-catalysed starch degradation and modification, there is considerable interest in how different alpha-amylases might accommodate these branches, thus impacting on the potential processing of highly branched post-hydrolysis remnants (known as limit dextrins) and societal applications. Here, it was sought to probe the branch-point accommodation of the Alicyclobacillus sp. CAZy family GH13 alpha-amylase AliC, prompted by the observation of a molecule of glucose in a position that may represent a branch point in an acarbose complex solved at 2.1 A resolution. Limit digest analysis by two-dimensional NMR using both pullulan (a regular linear polysaccharide of alpha-1,4, alpha-1,4, alpha-1,6 repeating trisaccharides) and amylopectin starch showed how the Alicyclobacillus sp. enzyme could accept alpha-1,6 branches in at least the -2, +1 and +2 subsites, consistent with the three-dimensional structures with glucosyl moieties in the +1 and +2 subsites and the solvent-exposure of the -2 subsite 6-hydroxyl group. Together, the work provides a rare insight into branch-point acceptance in these industrial catalysts.

The structure of the AliC GH13 alpha-amylase from Alicyclobacillus sp. reveals the accommodation of starch branching points in the alpha-amylase family.,Agirre J, Moroz O, Meier S, Brask J, Munch A, Hoff T, Andersen C, Wilson KS, Davies GJ Acta Crystallogr D Struct Biol. 2019 Jan 1;75(Pt 1):1-7. doi:, 10.1107/S2059798318014900. Epub 2019 Jan 4. PMID:30644839<ref>PMID:30644839</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6gya" style="background-color:#fffaf0;"></div>

==See Also==
*[[Amylase|Amylase]]
*[[Amylase 3D structures|Amylase 3D structures]]
*[[Journal:Acta Cryst D:S2059798318014900|Journal:Acta Cryst D:S2059798318014900]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alicyclobacillus sp]]
[[Category: Large Structures]]
[[Category: Agirre, J]]
[[Category: Andersen, C]]
[[Category: Brask, J]]
[[Category: Davies, G J]]
[[Category: Hoff, T]]
[[Category: Meier, S]]
[[Category: Moroz, O]]
[[Category: Munch, A]]
[[Category: Wilson, K S]]
[[Category: Amylase glycoside hydrolase]]
[[Category: Hydrolase]]