5zcd

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m (Protected "5zcd" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5zcd is ON HOLD until Paper Publication
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==Crystal structure of Alpha-glucosidase in complex with maltotriose==
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<StructureSection load='5zcd' size='340' side='right' caption='[[5zcd]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5zcd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZCD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZCD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MLR:MALTOTRIOSE'>MLR</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zcb|5zcb]], [[5zcc|5zcc]]</td></tr>
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<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=5zcd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zcd OCA], [http://pdbe.org/5zcd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zcd RCSB], [http://www.ebi.ac.uk/pdbsum/5zcd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zcd ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5zcd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Kato, K]]
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[[Category: Saburi, W]]
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[[Category: Yao, M]]
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[[Category: Alpha-glucosidase]]
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[[Category: Hydrolase]]

Revision as of 08:12, 26 December 2018

Crystal structure of Alpha-glucosidase in complex with maltotriose

5zcd, resolution 1.71Å

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