4mad: Difference between revisions
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==Crystal structure of beta-galactosidase C (BgaC) from Bacillus circulans ATCC 31382== | |||
<StructureSection load='4mad' size='340' side='right'caption='[[4mad]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mad]] is a 2 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=4MAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MAD 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</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=4mad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mad OCA], [https://pdbe.org/4mad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mad RCSB], [https://www.ebi.ac.uk/pdbsum/4mad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mad ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O31341_NIACI O31341_NIACI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of beta-galactosidase from Bacillus circulans (BgaC) was determined at 1.8A resolution. The overall structure of BgaC consists of three distinct domains, which are the catalytic domain with a TIM-barrel structure and two all-beta domains (ABDs). The main-chain fold and steric configurations of the acidic and aromatic residues at the active site were very similar to those of Streptococcus pneumoniae beta(1,3)-galactosidase BgaC in complex with galactose. The structure of BgaC was used for the rational design of a glycosynthase. BgaC belongs to the glycoside hydrolase family 35. The essential nucleophilic amino acid residue has been identified as glutamic acid at position 233 by site-directed mutagenesis. Construction of the active site mutant BgaC-Glu233Gly gave rise to a galactosynthase transferring the sugar moiety from alpha-d-galactopyranosyl fluoride (alphaGalF) to different beta-linked N-acetylglucosamine acceptor substrates in good yield (40-90%) with a remarkably stable product formation. Enzymatic syntheses with BgaC-Glu233Gly afforded the stereo- and regioselective synthesis of beta1-3-linked key galactosides like galacto-N-biose or lacto-N-biose. | |||
Rational design of a glycosynthase by the crystal structure of beta-galactosidase from Bacillus circulans (BgaC) and its use for the synthesis of N-acetyllactosamine type 1 glycan structures.,Henze M, You DJ, Kamerke C, Hoffmann N, Angkawidjaja C, Ernst S, Pietruszka J, Kanaya S, Elling L J Biotechnol. 2014 Jul 14. pii: S0168-1656(14)00337-X. doi:, 10.1016/j.jbiotec.2014.07.003. PMID:25034434<ref>PMID:25034434</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4mad" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galactosidase 3D structures|Galactosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Niallia circulans]] | |||
[[Category: Elling L]] | |||
[[Category: Kamerke C]] | |||
[[Category: Kanaya S]] | |||
[[Category: You DJ]] | |||
Latest revision as of 17:42, 8 November 2023
Crystal structure of beta-galactosidase C (BgaC) from Bacillus circulans ATCC 31382Crystal structure of beta-galactosidase C (BgaC) from Bacillus circulans ATCC 31382
Structural highlights
FunctionPublication Abstract from PubMedThe crystal structure of beta-galactosidase from Bacillus circulans (BgaC) was determined at 1.8A resolution. The overall structure of BgaC consists of three distinct domains, which are the catalytic domain with a TIM-barrel structure and two all-beta domains (ABDs). The main-chain fold and steric configurations of the acidic and aromatic residues at the active site were very similar to those of Streptococcus pneumoniae beta(1,3)-galactosidase BgaC in complex with galactose. The structure of BgaC was used for the rational design of a glycosynthase. BgaC belongs to the glycoside hydrolase family 35. The essential nucleophilic amino acid residue has been identified as glutamic acid at position 233 by site-directed mutagenesis. Construction of the active site mutant BgaC-Glu233Gly gave rise to a galactosynthase transferring the sugar moiety from alpha-d-galactopyranosyl fluoride (alphaGalF) to different beta-linked N-acetylglucosamine acceptor substrates in good yield (40-90%) with a remarkably stable product formation. Enzymatic syntheses with BgaC-Glu233Gly afforded the stereo- and regioselective synthesis of beta1-3-linked key galactosides like galacto-N-biose or lacto-N-biose. Rational design of a glycosynthase by the crystal structure of beta-galactosidase from Bacillus circulans (BgaC) and its use for the synthesis of N-acetyllactosamine type 1 glycan structures.,Henze M, You DJ, Kamerke C, Hoffmann N, Angkawidjaja C, Ernst S, Pietruszka J, Kanaya S, Elling L J Biotechnol. 2014 Jul 14. pii: S0168-1656(14)00337-X. doi:, 10.1016/j.jbiotec.2014.07.003. PMID:25034434[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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