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| | <StructureSection load='4hd6' size='340' side='right'caption='[[4hd6]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4hd6' size='340' side='right'caption='[[4hd6]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hd6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HD6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hd6]] 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=4HD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HD6 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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hda|4hda]], [[4hd4|4hd4]], [[4hd7|4hd7]]</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/Tyrosinase Tyrosinase], 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=4hd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hd6 OCA], [https://pdbe.org/4hd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hd6 RCSB], [https://www.ebi.ac.uk/pdbsum/4hd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hd6 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=4hd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hd6 OCA], [http://pdbe.org/4hd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hd6 RCSB], [http://www.ebi.ac.uk/pdbsum/4hd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hd6 ProSAT]</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>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4hd6" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Tyrosinase|Tyrosinase]] | + | *[[Tyrosinase 3D structures|Tyrosinase 3D structures]] |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 14581]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tyrosinase]] | + | [[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]]
| + | |
| - | [[Category: Type 3 copper protein]]
| + | |
