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8oi4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Metagenomic Beta-galactosidase from Glycoside Hydrolase family GH154== | |
| + | <StructureSection load='8oi4' size='340' side='right'caption='[[8oi4]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8oi4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Organismal_metagenomes Organismal metagenomes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OI4 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]] 1.76Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8oi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oi4 OCA], [https://pdbe.org/8oi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oi4 RCSB], [https://www.ebi.ac.uk/pdbsum/8oi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oi4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polysaccharide Utilization Loci (PULs) are physically linked gene clusters conserved in the Gram-negative phylum of Bacteroidota and are valuable sources for Carbohydrate Active enZyme (CAZyme) discovery. This study focuses on BD-beta-Gal, an enzyme encoded in a metagenomic PUL and member of the Glycoside Hydrolase family 154 (GH154). BD-beta-Gal showed exo-beta-galactosidase activity with regiopreference for hydrolyzing beta-d-(1,6) glycosidic linkages. Notably, it exhibited a preference for d-glucopyranosyl (d-Glcp) over d-galactopyranosyl (d-Galp) and d-fructofuranosyl (d-Fruf) at the reducing end of the investigated disaccharides. In addition, we determined the high resolution crystal structure of BD-beta-Gal, thus providing the first structural characterization of a GH154 enzyme. Surprisingly, this revealed an (alpha/alpha)(6) topology, which has not been observed before for beta-galactosidases. BD-beta-Gal displayed low structural homology with characterized CAZymes, but conservation analysis suggested that the active site was located in a central cavity, with conserved E73, R252, and D253 as putative catalytic residues. Interestingly, BD-beta-Gal has a tetrameric structure and a flexible loop from a neighboring protomer may contribute to its reaction specificity. Finally, we showed that the founding member of GH154, BT3677 from Bacteroides thetaiotaomicron, described as beta-glucuronidase, displayed exo-beta-galactosidase activity like BD-beta-Gal but lacked a tetrameric structure. | ||
| - | + | Novel beta-galactosidase activity and first crystal structure of Glycoside Hydrolase family 154.,Hameleers L, Pijning T, Gray BB, Faure R, Jurak E N Biotechnol. 2023 Dec 30;80:1-11. doi: 10.1016/j.nbt.2023.12.011. PMID:38163476<ref>PMID:38163476</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8oi4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Organismal metagenomes]] | ||
| + | [[Category: Guskov A]] | ||
| + | [[Category: Hameleers L]] | ||
| + | [[Category: Jurak E]] | ||
| + | [[Category: Pijning T]] | ||
Current revision
Metagenomic Beta-galactosidase from Glycoside Hydrolase family GH154
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