6m55: Difference between revisions
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==Crystal structure of the E496A mutant of HsBglA in complex with 4-galactosyllactose== | |||
<StructureSection load='6m55' size='340' side='right'caption='[[6m55]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M55 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]] 3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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=6m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m55 OCA], [https://pdbe.org/6m55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m55 RCSB], [https://www.ebi.ac.uk/pdbsum/6m55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m55 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 6m55" style="background-color:#fffaf0;"></div> | |||
== 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 08:07, 17 October 2024
Crystal structure of the E496A mutant of HsBglA in complex with 4-galactosyllactose
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