4mad

<StructureSection load='4mad' size='340' side='right'caption='[[4mad]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[4mad]] is a 2 chain structure. 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='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>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 4mad" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Hydrolase]]

[[Category: Elling, L]]

[[Category: Kamerke, C]]

[[Category: Kanaya, S]]

[[Category: You, D J]]

[[Category: Gh-a]]