4mad: Difference between revisions
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<StructureSection load='4mad' size='340' side='right' caption='[[4mad]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4mad' size='340' side='right' caption='[[4mad]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MAD FirstGlance]. <br> | <table><tr><td colspan='2'>[[4mad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_24 Atcc 24]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MAD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bgaC, D88750 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1397 ATCC 24])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mad OCA], [http://pdbe.org/4mad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mad RCSB], [http://www.ebi.ac.uk/pdbsum/4mad PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mad ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mad OCA], [http://pdbe.org/4mad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mad RCSB], [http://www.ebi.ac.uk/pdbsum/4mad PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mad ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 24]] | |||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Elling, L]] | [[Category: Elling, L]] | ||
Revision as of 12:48, 15 November 2017
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
Publication 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. References
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