View source for 5zcc


==Crystal structure of Alpha-glucosidase in complex with maltose==
<StructureSection load='5zcc' size='340' side='right'caption='[[5zcc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zcc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._(in:_Bacteria) Bacillus sp. (in: Bacteria)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZCC 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]] 1.704&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=5zcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zcc OCA], [https://pdbe.org/5zcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zcc RCSB], [https://www.ebi.ac.uk/pdbsum/5zcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zcc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2Z5WH92_BACSP A0A2Z5WH92_BACSP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-Glucosidase hydrolyzes alpha-glucosides and transfers alpha-glucosyl residues to an acceptor through transglucosylation. In this study, GH13_31 alpha-glucosidase BspAG13_31A with high transglucosylation activity is reported in Bacillus sp. AHU2216 and biochemically and structurally characterized. This enzyme is specific to alpha-(1--&gt;4)-glucosidic linkage as substrates and transglucosylation products. Maltose is the most preferred substrate. Crystal structures of BspAG13_31A wild-type for the substrate-free form and inactive acid/base mutant E256Q in complexes with maltooligosaccharides were solved at 1.6-2.5 A resolution. BspAG13_31A has a catalytic domain folded by an (beta/alpha)8 -barrel. In subsite +1, Ala200 and His203 on beta--&gt;alpha loop 4 and Asn258 on beta--&gt;alpha loop 5 are involved in the recognition of maltooligosaccharides. Structural basis for specificity of GH13_31 enzymes to alpha-(1--&gt;4)-glucosidic linkage is first described.

Function and structure of GH13_31 alpha-glucosidase with high alpha-(1--&gt;4)-glucosidic linkage specificity and transglucosylation activity.,Auiewiriyanukul W, Saburi W, Kato K, Yao M, Mori H FEBS Lett. 2018 Jul;592(13):2268-2281. doi: 10.1002/1873-3468.13126. Epub 2018, Jun 20. PMID:29870070<ref>PMID:29870070</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zcc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Kato K]]
[[Category: Saburi W]]
[[Category: Yao M]]