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| | <StructureSection load='1wx5' size='340' side='right'caption='[[1wx5]], [[Resolution|resolution]] 2.02Å' scene=''> | | <StructureSection load='1wx5' size='340' side='right'caption='[[1wx5]], [[Resolution|resolution]] 2.02Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wx5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_castaneoglobisporus"_yen "actinomyces castaneoglobisporus" yen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WX5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1WX5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1wx5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_castaneoglobisporus Streptomyces castaneoglobisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WX5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.02Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wx2|1wx2]], [[1wx3|1wx3]], [[1wx4|1wx4]], [[1wxc|1wxc]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tyrc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 "Actinomyces castaneoglobisporus" Yen]), orf378 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 "Actinomyces castaneoglobisporus" Yen])</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=1wx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wx5 OCA], [https://pdbe.org/1wx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wx5 RCSB], [https://www.ebi.ac.uk/pdbsum/1wx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wx5 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/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'>[http://proteopedia.org/fgij/fg.htm?mol=1wx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wx5 OCA], [http://pdbe.org/1wx5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wx5 RCSB], [http://www.ebi.ac.uk/pdbsum/1wx5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wx5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q83WS2_9ACTN Q83WS2_9ACTN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces castaneoglobisporus yen]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tyrosinase]] | + | [[Category: Streptomyces castaneoglobisporus]] |
| - | [[Category: Kumagai, T]] | + | [[Category: Kumagai T]] |
| - | [[Category: Matoba, Y]] | + | [[Category: Matoba Y]] |
| - | [[Category: Sugiyama, M]] | + | [[Category: Sugiyama M]] |
| - | [[Category: Yamamoto, A]] | + | [[Category: Yamamoto A]] |
| - | [[Category: Yoshitsu, H]] | + | [[Category: Yoshitsu H]] |
| - | [[Category: Binary complex]]
| + | |
| - | [[Category: Flexibility]]
| + | |
| - | [[Category: Oxidoreductase-metal transport complex]]
| + | |
| Structural highlights
Function
Q83WS2_9ACTN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
At high resolution, we determined the crystal structures of copper-bound and metal-free tyrosinase in a complex with ORF378 designated as a "caddie" protein because it assists with transportation of two CuII ions into the tyrosinase catalytic center. These structures suggest that the caddie protein covers the hydrophobic molecular surface of tyrosinase and interferes with the binding of a substrate tyrosine to the catalytic site of tyrosinase. The caddie protein, which consists of one six-strandedbeta-sheet and one alpha-helix, has no similarity with all proteins deposited into the Protein Data Bank. Although tyrosinase and catechol oxidase are classified into the type 3 copper protein family, the latter enzyme lacks monooxygenase activity. The difference in catalytic activity is based on the structural observations that a large vacant space is present just above the active center of tyrosinase and that one of the six His ligands for the two copper ions is highly flexible. These structural characteristics of tyrosinase suggest that, in the reaction that catalyzes the ortho-hydroxylation of monophenol, one of the two Cu(II) ions is coordinated by the peroxide-originated oxygen bound to the substrate. Our crystallographic study shows evidence that the tyrosinase active center formed by dinuclear coppers is flexible during catalysis.
Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis.,Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M J Biol Chem. 2006 Mar 31;281(13):8981-90. Epub 2006 Jan 25. PMID:16436386[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J Biol Chem. 2006 Mar 31;281(13):8981-90. Epub 2006 Jan 25. PMID:16436386 doi:10.1074/jbc.M509785200
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