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==Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularis== | |||
<StructureSection load='6m4e' size='340' side='right'caption='[[6m4e]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M4E 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6m4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m4e OCA], [https://pdbe.org/6m4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m4e RCSB], [https://www.ebi.ac.uk/pdbsum/6m4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m4e ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A GH1 beta-glucosidase from the fungus Hamamotoa singularis (HsBglA) has high transgalactosylation activity and efficiently converts lactose to galactooligosaccharides. Consequently, HsBglA is among the most widely used enzymes for industrial galactooligosaccharide production. Here, we present the first crystal structures of HsBglA with and without 4'-galactosyllactose, a tri-galactooligosaccharide, at 3.0 and 2.1 A resolutions, respectively. These structures reveal details of the structural elements that define the catalytic activity and substrate binding of HsBglA, and provide a possible interpretation for its high catalytic potency for transgalactosylation reaction. | |||
Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularis.,Uehara R, Iwamoto R, Aoki S, Yoshizawa T, Takano K, Matsumura H, Tanaka SI Protein Sci. 2020 Jul 26. doi: 10.1002/pro.3916. PMID:32713015<ref>PMID:32713015</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6m4e" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galactosidase 3D structures|Galactosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Aoki S]] | |||
[[Category: Iwamoto R]] | |||
[[Category: Matsumura H]] | |||
[[Category: Takano K]] | |||
[[Category: Tanaka S-i]] | |||
[[Category: Uehara R]] | |||
[[Category: Yoshizawa T]] | |||
Latest revision as of 14:11, 30 October 2024
Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularisCrystal structure of a GH1 beta-glucosidase from Hamamotoa singularis
Structural highlights
Publication Abstract from PubMedA GH1 beta-glucosidase from the fungus Hamamotoa singularis (HsBglA) has high transgalactosylation activity and efficiently converts lactose to galactooligosaccharides. Consequently, HsBglA is among the most widely used enzymes for industrial galactooligosaccharide production. Here, we present the first crystal structures of HsBglA with and without 4'-galactosyllactose, a tri-galactooligosaccharide, at 3.0 and 2.1 A resolutions, respectively. These structures reveal details of the structural elements that define the catalytic activity and substrate binding of HsBglA, and provide a possible interpretation for its high catalytic potency for transgalactosylation reaction. Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularis.,Uehara R, Iwamoto R, Aoki S, Yoshizawa T, Takano K, Matsumura H, Tanaka SI Protein Sci. 2020 Jul 26. doi: 10.1002/pro.3916. PMID:32713015[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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