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| ==Crystal Structure of Tyrosinase from Bacillus megaterium V218G mutant soaked in CuSO4== | | ==Crystal Structure of Tyrosinase from Bacillus megaterium V218G mutant soaked in CuSO4== |
| <StructureSection load='4hd7' size='340' side='right' caption='[[4hd7]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4hd7' size='340' side='right'caption='[[4hd7]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4hd7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HD7 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4hd7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HD7 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]] 2.1Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hda|4hda]], [[4hd4|4hd4]], [[4hd6|4hd6]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monophenol_monooxygenase Monophenol monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.18.1 1.14.18.1] </span></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=4hd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hd7 OCA], [https://pdbe.org/4hd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hd7 RCSB], [https://www.ebi.ac.uk/pdbsum/4hd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hd7 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=4hd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hd7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hd7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hd7 PDBsum]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/B2ZB02_PRIMG B2ZB02_PRIMG] |
| Tyrosinase is a type 3 copper enzyme with great potential for production of commercially valuable diphenols from monophenols. However, the use of tyrosinase is limited by its further oxidation of diphenols to quinones. We recently determined the structure of the Bacillus megaterium tyrosinase revealing a residue, V218, which we proposed to take part in positioning of substrates within the active site. In the structure of catechol oxidase from Ipomoea batatas, the lack of monophenolase activity was attributed to the presence of F261 near CuA. Consequently, we engineered two variants, V218F and V218G. V218F was expected to have a decreased monophenolase activity, due to the bulky residue extending into the active site. Surprisingly, both V218F and V218G exhibited a 9- and 4.4-fold higher monophenolase/diphenolase activity ratio, respectively. X-ray structures of variant V218F display a flexibility of the phenylalanine residue along with an adjacent histidine, which we propose to be the source of the change in activity ratio.
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| Influencing the monophenolase/diphenolase activity ratio in tyrosinase.,Goldfeder M, Kanteev M, Adir N, Fishman A Biochim Biophys Acta. 2013 Jan 8. pii: S1570-9639(13)00003-4. doi:, 10.1016/j.bbapap.2012.12.021. PMID:23305929<ref>PMID:23305929</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | ==See Also== |
| </div>
| | *[[Tyrosinase 3D structures|Tyrosinase 3D structures]] |
| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus megaterium]] | | [[Category: Large Structures]] |
| [[Category: Monophenol monooxygenase]] | | [[Category: Priestia megaterium]] |
| [[Category: Adir, N]] | | [[Category: Adir N]] |
| [[Category: Fishman, A]] | | [[Category: Fishman A]] |
| [[Category: Goldfeder, M]] | | [[Category: Goldfeder M]] |
| [[Category: Kanteev, M]] | | [[Category: Kanteev M]] |
| [[Category: Oxidoreductase]]
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| [[Category: Type 3 copper protein]]
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| [[Category: Tyrosinase]]
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