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| | <StructureSection load='3w6q' size='340' side='right'caption='[[3w6q]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='3w6q' size='340' side='right'caption='[[3w6q]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3w6q]] is a 4 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=3W6Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W6Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w6q]] is a 4 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=3W6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W6Q FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w6w|3w6w]]</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]] 2.052Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">melB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5062 ASPOZ])</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=3w6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6q OCA], [https://pdbe.org/3w6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w6q RCSB], [https://www.ebi.ac.uk/pdbsum/3w6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w6q 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=3w6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6q OCA], [http://pdbe.org/3w6q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3w6q RCSB], [http://www.ebi.ac.uk/pdbsum/3w6q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3w6q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q2UP46_ASPOR Q2UP46_ASPOR] Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate.[ARBA:ARBA00003864] |
| - | Tyrosinase, a dinuclear copper monooxygenase/oxidase, plays a crucial role in the melanin pigment biosynthesis. The structure and functions of tyrosinase have so far been studied extensively, but the post-translational maturation process from the pro-form to the active form has been less explored. In this study, we provide the crystal structures of Aspergillus oryzae full-length pro-tyrosinase in the holo- and the apo-forms at 1.39 and 2.05 A resolution, respectively, revealing that Phe(513) on the C-terminal domain is accommodated in the substrate-binding site as a substrate analog to protect the dicopper active site from substrate access (proteolytic cleavage of the C-terminal domain or deformation of the C-terminal domain by acid treatment transforms the pro-tyrosinase to the active enzyme (Fujieda, N., Murata, M., Yabuta, S., Ikeda, T., Shimokawa, C., Nakamura, Y., Hata, Y., and Itoh, S. (2012) ChemBioChem. 13, 193-201 and Fujieda, N., Murata, M., Yabuta, S., Ikeda, T., Shimokawa, C., Nakamura, Y., Hata, Yl, and Itoh, S. (2013) J. Biol. Inorg. Chem. 18, 19-26). Detailed crystallographic analysis and structure-based mutational studies have shown that the copper incorporation into the active site is governed by three cysteines as follows: Cys(92), which is covalently bound to His(94) via an unusual thioether linkage in the holo-form, and Cys(522) and Cys(525) of the CXXC motif located on the C-terminal domain. Molecular mechanisms of the maturation processes of fungal tyrosinase involving the accommodation of the dinuclear copper unit, the post-translational His-Cys thioether cross-linkage formation, and the proteolytic C-terminal cleavage to produce the active tyrosinase have been discussed on the basis of the detailed structural information.
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| - | Crystal structures of copper-depleted and copper-bound fungal pro-tyrosinase: insights into endogenous cysteine-dependent copper incorporation.,Fujieda N, Yabuta S, Ikeda T, Oyama T, Muraki N, Kurisu G, Itoh S J Biol Chem. 2013 Jul 26;288(30):22128-40. doi: 10.1074/jbc.M113.477612. Epub, 2013 Jun 7. PMID:23749993<ref>PMID:23749993</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 3w6q" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Tyrosinase|Tyrosinase]] | + | *[[Tyrosinase 3D structures|Tyrosinase 3D structures]] |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspoz]] | + | [[Category: Aspergillus oryzae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fujieda, N]] | + | [[Category: Fujieda N]] |
| - | [[Category: Ikeda, T]] | + | [[Category: Ikeda T]] |
| - | [[Category: Itoh, S]] | + | [[Category: Itoh S]] |
| - | [[Category: Kurisu, G]] | + | [[Category: Kurisu G]] |
| - | [[Category: Muraki, N]] | + | [[Category: Muraki N]] |
| - | [[Category: Oyama, T]] | + | [[Category: Oyama T]] |
| - | [[Category: Yabuta, S]] | + | [[Category: Yabuta S]] |
| - | [[Category: Four helix bundle]]
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| - | [[Category: Metal binding protein]]
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| - | [[Category: Oxidoreductase]]
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