View source for 7dcg


==Alpha-glucosidase from Weissella cibaria BBK-1 bound with maltotriose==
<StructureSection load='7dcg' size='340' side='right'caption='[[7dcg]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7dcg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Weissella_cibaria Weissella cibaria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DCG 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]] 1.53&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7dcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dcg OCA], [https://pdbe.org/7dcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dcg RCSB], [https://www.ebi.ac.uk/pdbsum/7dcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dcg ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
alpha-Glucosidase (EC 3.2.1.20) is a carbohydrate-hydrolyzing enzyme which generally cleaves alpha-1,4-glycosidic bonds of oligosaccharides and starch from the nonreducing ends. In this study, the novel alpha-glucosidase from Weissella cibaria BBK-1 (WcAG) was biochemically and structurally characterized. WcAG belongs to glycoside hydrolase family 13 (GH13) and to the neopullanase subfamily. It exhibits distinct hydrolytic activity towards the alpha-1,4 linkages of short-chain oligosaccharides from the reducing end. The enzyme prefers to hydrolyse maltotriose and acarbose, while it cannot hydrolyse cyclic oligosaccharides and polysaccharides. In addition, WcAG can cleave pullulan hydrolysates and strongly exhibits transglycosylation activity in the presence of maltose. Size-exclusion chromatography and X-ray crystal structures revealed that WcAG forms a homodimer in which the N-terminal domain of one monomer is orientated in proximity to the catalytic domain of another, creating the substrate-binding groove. Crystal structures of WcAG in complexes with maltose, maltotriose and acarbose revealed a remarkable enzyme active site with accessible +2, +1 and -1 subsites, along with an Arg-Glu gate (Arg176-Glu296) in front of the active site. The -2 and -3 subsites were blocked by Met119 and Asn120 from the N-terminal domain of a different subunit, resulting in an extremely restricted substrate preference.

A GH13 alpha-glucosidase from Weissella cibaria uncommonly acts on short-chain maltooligosaccharides.,Wangpaiboon K, Laohawuttichai P, Kim SY, Mori T, Nakapong S, Pichyangkura R, Pongsawasdi P, Hakoshima T, Krusong K Acta Crystallogr D Struct Biol. 2021 Aug 1;77(Pt 8):1064-1076. doi:, 10.1107/S205979832100677X. Epub 2021 Jul 29. PMID:34342279<ref>PMID:34342279</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Weissella cibaria]]
[[Category: Hakoshima T]]
[[Category: Kim S]]
[[Category: Krusong K]]
[[Category: Mori T]]
[[Category: Wangpaiboon K]]