5zcc: Difference between revisions
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==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 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]] 1.704Å</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-->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> | |||
==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]] | |||
Latest revision as of 11:51, 22 November 2023
Crystal structure of Alpha-glucosidase in complex with maltoseCrystal structure of Alpha-glucosidase in complex with maltose
Structural highlights
FunctionPublication Abstract from PubMedalpha-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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