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5zcc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Alpha-glucosidase in complex with maltose== | |
| + | <StructureSection load='5zcc' size='340' side='right' caption='[[5zcc]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5zcc]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZCC FirstGlance]. <br> | ||
| + | </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=MAL:MALTOSE'>MAL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zcb|5zcb]]</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=5zcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zcc OCA], [http://pdbe.org/5zcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zcc RCSB], [http://www.ebi.ac.uk/pdbsum/5zcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zcc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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-->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-->alpha loop 4 and Asn258 on beta-->alpha loop 5 are involved in the recognition of maltooligosaccharides. Structural basis for specificity of GH13_31 enzymes to alpha-(1-->4)-glucosidic linkage is first described. | ||
| - | + | Function and structure of GH13_31 alpha-glucosidase with high alpha-(1-->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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5zcc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kato, K]] | ||
| + | [[Category: Saburi, W]] | ||
| + | [[Category: Yao, M]] | ||
| + | [[Category: Alpha-glucosidase]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 08:12, 26 December 2018
Crystal structure of Alpha-glucosidase in complex with maltose
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