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==Crystal structure of beta-galactosidase II from Bacillus circulans in complex with beta-D-galactopyranosyl disaccharide== | ==Crystal structure of beta-galactosidase II from Bacillus circulans in complex with beta-D-galactopyranosyl disaccharide== | ||
<StructureSection load='7cwd' size='340' side='right'caption='[[7cwd]]' scene=''> | <StructureSection load='7cwd' size='340' side='right'caption='[[7cwd]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CWD OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[7cwd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CWD FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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></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=7cwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cwd OCA], [https://pdbe.org/7cwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cwd RCSB], [https://www.ebi.ac.uk/pdbsum/7cwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cwd ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A6M5K904_NIACI A0A6M5K904_NIACI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The transgalactosylase activity of beta-galactosidase produces galacto-oligosaccharides (GOSs) with prebiotic effects similar to those of major oligosaccharides in human milk. beta-Galactosidases from Bacillus circulans ATCC 31382 are important enzymes in industrial-scale GOS production. Here, we show the high GOS yield of beta-galactosidase II from B. circulans (beta-Gal-II, Lactazyme-B), compared to other commercial enzymes. We also determine the crystal structure of the five conserved domains of beta-Gal-II in an apo-form and complexed with galactose and an acceptor sugar, showing the heterogeneous mode of transgalactosylation by the enzyme. Truncation studies of the five conserved domains reveal that all five domains are essential for enzyme catalysis, while some truncated constructs were still expressed as soluble proteins. Structural comparison of beta-Gal-II with other beta-galactosidase homologues suggests that the GOS linkage preference of the enzyme might be quite different from other enzymes. The structural information on beta-Gal-II might provide molecular insights into the transgalactosylation process of the beta-galactosidases in GOS production. | |||
High Galacto-Oligosaccharide Production and a Structural Model for Transgalactosylation of beta-Galactosidase II from Bacillus circulans.,Choi JY, Hong H, Seo H, Pan JG, Kim EJ, Maeng PJ, Yang TH, Kim KJ J Agric Food Chem. 2020 Nov 25;68(47):13806-13814. doi: 10.1021/acs.jafc.0c05871., Epub 2020 Nov 10. PMID:33169609<ref>PMID:33169609</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7cwd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galactosidase 3D structures|Galactosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Niallia circulans]] | |||
[[Category: Hong H]] | [[Category: Hong H]] | ||
[[Category: Seo H]] | [[Category: Seo H]] |
Latest revision as of 19:17, 29 November 2023
Crystal structure of beta-galactosidase II from Bacillus circulans in complex with beta-D-galactopyranosyl disaccharideCrystal structure of beta-galactosidase II from Bacillus circulans in complex with beta-D-galactopyranosyl disaccharide
Structural highlights
FunctionPublication Abstract from PubMedThe transgalactosylase activity of beta-galactosidase produces galacto-oligosaccharides (GOSs) with prebiotic effects similar to those of major oligosaccharides in human milk. beta-Galactosidases from Bacillus circulans ATCC 31382 are important enzymes in industrial-scale GOS production. Here, we show the high GOS yield of beta-galactosidase II from B. circulans (beta-Gal-II, Lactazyme-B), compared to other commercial enzymes. We also determine the crystal structure of the five conserved domains of beta-Gal-II in an apo-form and complexed with galactose and an acceptor sugar, showing the heterogeneous mode of transgalactosylation by the enzyme. Truncation studies of the five conserved domains reveal that all five domains are essential for enzyme catalysis, while some truncated constructs were still expressed as soluble proteins. Structural comparison of beta-Gal-II with other beta-galactosidase homologues suggests that the GOS linkage preference of the enzyme might be quite different from other enzymes. The structural information on beta-Gal-II might provide molecular insights into the transgalactosylation process of the beta-galactosidases in GOS production. High Galacto-Oligosaccharide Production and a Structural Model for Transgalactosylation of beta-Galactosidase II from Bacillus circulans.,Choi JY, Hong H, Seo H, Pan JG, Kim EJ, Maeng PJ, Yang TH, Kim KJ J Agric Food Chem. 2020 Nov 25;68(47):13806-13814. doi: 10.1021/acs.jafc.0c05871., Epub 2020 Nov 10. PMID:33169609[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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