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| | <StructureSection load='6ju7' size='340' side='right'caption='[[6ju7]], [[Resolution|resolution]] 1.42Å' scene=''> | | <StructureSection load='6ju7' size='340' side='right'caption='[[6ju7]], [[Resolution|resolution]] 1.42Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ju7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspoz Aspoz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JU7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JU7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ju7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JU7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=TYR:TYROSINE'>TYR</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]] 1.42Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OAory_01107480 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5062 ASPOZ])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=TYR:TYROSINE'>TYR</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=6ju7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ju7 OCA], [https://pdbe.org/6ju7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ju7 RCSB], [https://www.ebi.ac.uk/pdbsum/6ju7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ju7 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ju7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ju7 OCA], [http://pdbe.org/6ju7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ju7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ju7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ju7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1S9DK56_ASPOZ A0A1S9DK56_ASPOZ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspoz]] | + | [[Category: Aspergillus oryzae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tyrosinase]]
| + | [[Category: Fujieda N]] |
| - | [[Category: Fujieda, N]] | + | [[Category: Itoh S]] |
| - | [[Category: Itoh, S]] | + | [[Category: Kurisu G]] |
| - | [[Category: Kurisu, G]] | + | [[Category: Nishikawa Y]] |
| - | [[Category: Nishikawa, Y]] | + | [[Category: Umakoshi K]] |
| - | [[Category: Umakoshi, K]] | + | |
| - | [[Category: Copper enzyme]]
| + | |
| - | [[Category: Dinuclear copper center]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
A0A1S9DK56_ASPOZ
Publication Abstract from PubMed
The dinuclear copper enzyme tyrosinase activates O2 to form a (mu-eta2:eta2-peroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate. We herein report the near atomic resolution X-ray crystal structures of the active tyrosinases with substrate L-tyrosine. At their catalytic sites, CuA moved largely toward L-tyrosine (CuA1 to CuA2), whose phenol oxygen directly coordinates to CuA2, involving the movement of CuB (CuB1 to CuB2). The crystal structures and spectroscopic analyses of the dioxygen-bound tyrosinases demonstrated that the peroxide ligand rotated, spontaneously weakening its O-O bond. Thus, the copper migration induced by the substrate-binding accompanied rearrangement of the bound peroxide species so as to facilitate one of the peroxide oxygen atoms to access to the phenol substrate's epsilon carbon atom.
Copper-oxygen Dynamics in Tyrosinase Mechanism.,Fujieda N, Umakoshi K, Ochi Y, Nishikawa Y, Yanagisawa S, Kubo M, Kurisu G, Itoh S Angew Chem Int Ed Engl. 2020 Apr 30. doi: 10.1002/anie.202004733. PMID:32356371[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujieda N, Umakoshi K, Ochi Y, Nishikawa Y, Yanagisawa S, Kubo M, Kurisu G, Itoh S. Copper-oxygen Dynamics in Tyrosinase Mechanism. Angew Chem Int Ed Engl. 2020 Apr 30. doi: 10.1002/anie.202004733. PMID:32356371 doi:http://dx.doi.org/10.1002/anie.202004733
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