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==Crystal structure of Alpha-glucosidase in complex with maltotriose==
==Crystal structure of Alpha-glucosidase in complex with maltotriose==
<StructureSection load='5zcd' size='340' side='right' caption='[[5zcd]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
<StructureSection load='5zcd' size='340' side='right'caption='[[5zcd]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[5zcd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsp Bacsp]. 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://proteopedia.org/fgij/fg.htm?mol=5ZCD 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=MLR:MALTOTRIOSE'>MLR</scene></td></tr>
</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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zcb|5zcb]], [[5zcc|5zcc]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zcb|5zcb]], [[5zcc|5zcc]]</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=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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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</div>
</div>
<div class="pdbe-citations 5zcd" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5zcd" style="background-color:#fffaf0;"></div>
==See Also==
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacsp]]
[[Category: Large Structures]]
[[Category: Kato, K]]
[[Category: Kato, K]]
[[Category: Saburi, W]]
[[Category: Saburi, W]]

Revision as of 00:18, 29 October 2020

Crystal structure of Alpha-glucosidase in complex with maltotrioseCrystal structure of Alpha-glucosidase in complex with maltotriose

Structural highlights

5zcd is a 1 chain structure with sequence from Bacsp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

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

5zcd, resolution 1.71Å

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