5z9s

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m (Protected "5z9s" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5z9s is ON HOLD
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==Functional and Structural Characterization of a beta-Glucosidase Involved in Saponin Metabolism from Intestinal Bacteria==
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<StructureSection load='5z9s' size='340' side='right' caption='[[5z9s]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5z9s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z9S FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr>
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<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=5z9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z9s OCA], [http://pdbe.org/5z9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z9s RCSB], [http://www.ebi.ac.uk/pdbsum/5z9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z9s ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Saponins are natural glycosides widely used in medicine and the food industry. Although saponin metabolism in human is dependent on intestinal microbes, few involving bacteria enzymes have been identified. We cloned BlBG3, a GH3 beta-glucosidase from Bifidobacterium longum, from human stool. We found that BlBG3 catalyzes the hydrolysis of glycoside furostanol and ginsenoside Rb1 at higher efficiency than other microbial beta-glucosidases. Structural analysis of BlBG3 in complex with d-glucose revealed its three unique loops, which form a deep pocket and participate in substrate binding. To understand how substrate is bound to the pocket, molecular docking was performed and the binding interactions of protobioside with BlBG3 were revealed. Mutational study suggested that R484 and H642 are critical for enzymatic activity. Our study presents the first structural and functional analysis of a saponin-processing enzyme from human microbiota.
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Authors: Yan, S., Wei, P.C., Li, J.R.
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Functional and structural characterization of a beta-glucosidase involved in saponin metabolism from intestinal bacteria.,Yan S, Wei PC, Chen Q, Chen X, Wang SC, Li JR, Gao C Biochem Biophys Res Commun. 2018 Feb 19;496(4):1349-1356. doi:, 10.1016/j.bbrc.2018.02.018. Epub 2018 Feb 5. PMID:29421652<ref>PMID:29421652</ref>
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Description: Functional and Structural Characterization of a beta-Glucosidase Involved in Saponin Metabolism from Intestinal Bacteria
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Wei, P.C]]
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<div class="pdbe-citations 5z9s" style="background-color:#fffaf0;"></div>
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[[Category: Li, J.R]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Li, J R]]
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[[Category: Wei, P C]]
[[Category: Yan, S]]
[[Category: Yan, S]]
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[[Category: Bifidobacterium longum]]
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[[Category: Biotransformation]]
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[[Category: Glucosidase]]
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[[Category: Hydrolase]]
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[[Category: Saponin]]

Revision as of 06:28, 14 March 2018

Functional and Structural Characterization of a beta-Glucosidase Involved in Saponin Metabolism from Intestinal Bacteria

5z9s, resolution 2.30Å

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