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| ==Pyranose 2-oxidase H167A mutant soaked with 3-fluorinated galactose (not bound)== | | ==Pyranose 2-oxidase H167A mutant soaked with 3-fluorinated galactose (not bound)== |
| <StructureSection load='4mok' size='340' side='right' caption='[[4mok]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4mok' size='340' side='right'caption='[[4mok]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4mok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Coriolus_zonatus Coriolus zonatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MOK FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4mok]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trametes_ochracea Trametes ochracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MOK FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tt0|1tt0]], [[2igo|2igo]], [[3pl8|3pl8]], [[4moe|4moe]], [[4mof|4mof]], [[4mog|4mog]], [[4moh|4moh]], [[4moi|4moi]], [[4moj|4moj]], [[4mol|4mol]], [[4mom|4mom]], [[4moo|4moo]], [[4mop|4mop]], [[4moq|4moq]], [[4mor|4mor]], [[4mos|4mos]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p2o ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230624 Coriolus zonatus])</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=4mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mok OCA], [https://pdbe.org/4mok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mok RCSB], [https://www.ebi.ac.uk/pdbsum/4mok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mok ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.10 1.1.3.10] </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=4mok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mok OCA], [http://pdbe.org/4mok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mok RCSB], [http://www.ebi.ac.uk/pdbsum/4mok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mok ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q7ZA32_TRAOC Q7ZA32_TRAOC] |
| Each year, about six million tons of lactose are generated from liquid whey as industrial byproduct, and optimally this large carbohydrate waste should be used for the production of value-added products. Trametes multicolor pyranose 2-oxidase (TmP2O) catalyzes the oxidation of various monosaccharides to the corresponding 2-keto sugars. Thus, a potential use of TmP2O is to convert the products from lactose hydrolysis, D-glucose and D-galactose, to more valuable products such as tagatose. Oxidation of glucose is however strongly favored over galactose, and oxidation of both substrates at more equal rates is desirable. Characterization of TmP2O variants (H450G, V546C, H450G/V546C) with improved D-galactose conversion has been given earlier, of which H450G displayed the best relative conversion between the substrates. To rationalize the changes in conversion rates, we have analyzed high-resolution crystal structures of the aforementioned mutants with bound 2- and 3-fluorinated glucose and galactose. Binding of glucose and galactose in the productive 2-oxidation binding mode is nearly identical in all mutants, suggesting that this binding mode is essentially unaffected by the mutations. For the competing glucose binding mode, enzyme variants carrying the H450G replacement stabilize glucose as the alpha-anomer in position for 3-oxidation. The backbone relaxation at position 450 allows the substrate-binding loop to fold tightly around the ligand. V546C however stabilize glucose as the beta-anomer using an open loop conformation. Improved binding of galactose is enabled by subtle relaxation effects at key active-site backbone positions. The competing binding mode for galactose 2-oxidation by V546C stabilizes the beta-anomer for oxidation at C1, whereas H450G variants stabilize the 3-oxidation binding mode of the galactose alpha-anomer. The present study provides a detailed description of binding modes that rationalize changes in the relative conversion rates of D-glucose and D-galactose and can be used to refine future enzyme designs for more efficient use of lactose-hydrolysis byproducts.
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| Structural Basis for Binding of Fluorinated Glucose and Galactose to Trametes multicolor Pyranose 2-Oxidase Variants with Improved Galactose Conversion.,Tan TC, Spadiut O, Gandini R, Haltrich D, Divne C PLoS One. 2014 Jan 21;9(1):e86736. doi: 10.1371/journal.pone.0086736. eCollection, 2014 Jan 21. PMID:24466218<ref>PMID:24466218</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4mok" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Pyranose oxidase|Pyranose oxidase]] | | *[[Pyranose oxidase|Pyranose oxidase]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Coriolus zonatus]] | | [[Category: Large Structures]] |
| [[Category: Pyranose oxidase]] | | [[Category: Trametes ochracea]] |
| [[Category: Divne, C]] | | [[Category: Divne C]] |
| [[Category: Gandini, R]] | | [[Category: Gandini R]] |
| [[Category: Haltrich, D]] | | [[Category: Haltrich D]] |
| [[Category: Spadiut, O]] | | [[Category: Spadiut O]] |
| [[Category: Tan, T C]] | | [[Category: Tan TC]] |
| [[Category: Fad-binding]]
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| [[Category: Flavinylation]]
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| [[Category: Gmc oxidoreductase]]
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| [[Category: Homotetramer]]
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| [[Category: Intracellular]]
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| [[Category: Oxidoreductase]]
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| [[Category: Phbh fold]]
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