3zph

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'''Unreleased structure'''
 
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The entry 3zph is ON HOLD
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==Bacterial chalcone isomerase in closed conformation from Eubacterium ramulus at 2.8 A resolution==
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<StructureSection load='3zph' size='340' side='right'caption='[[3zph]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3zph]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Eubacterium_ramulus Eubacterium ramulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZPH FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zph OCA], [https://pdbe.org/3zph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zph RCSB], [https://www.ebi.ac.uk/pdbsum/3zph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zph ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/U2Q8X2_EUBRA U2Q8X2_EUBRA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Flavonoids are a large group of plant secondary metabolites with a variety of biological properties and are therefore of interest to many scientists, as they can lead to industrially interesting intermediates. The anaerobic gut bacterium Eubacterium ramulus can catabolize flavonoids, but until now, the pathway has not been experimentally confirmed. In the present work, a chalcone isomerase (CHI) and an enoate reductase (ERED) could be identified through whole genome sequencing and gene motif search. These two enzymes were successfully cloned and expressed in Escherichia coli in their active form, even under aerobic conditions. The catabolic pathway of E. ramulus was confirmed by biotransformations of flavanones into dihydrochalcones. The engineered E. coli strain that expresses both enzymes was used for the conversion of several flavanones, underlining the applicability of this biocatalytic cascade reaction.
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Authors: Thomsen, M., Palm, G., Hinrichs, W.
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Enzymatic Conversion of Flavonoids using Bacterial Chalcone Isomerase and Enoate Reductase.,Gall M, Thomsen M, Peters C, Pavlidis IV, Jonczyk P, Grunert PP, Beutel S, Scheper T, Gross E, Backes M, Geissler T, Ley JP, Hilmer JM, Krammer G, Palm GJ, Hinrichs W, Bornscheuer UT Angew Chem Int Ed Engl. 2014 Jan 27;53(5):1439-42. doi: 10.1002/anie.201306952., Epub 2013 Dec 20. PMID:24459060<ref>PMID:24459060</ref>
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Description: Bacterial chalcone isomerase in closed conformation from Eubacterium ramulus at 2.8 A resolution
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3zph" style="background-color:#fffaf0;"></div>
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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: Eubacterium ramulus]]
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[[Category: Large Structures]]
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[[Category: Hinrichs W]]
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[[Category: Palm GJ]]
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[[Category: Thomsen M]]

Current revision

Bacterial chalcone isomerase in closed conformation from Eubacterium ramulus at 2.8 A resolution

PDB ID 3zph

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