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| | ==Crystal structure of Streptomyces tyrosinase in a complex with caddie soaked in a Cu(II)-containing solution for 80 hr: occupancy of CuA is low== | | ==Crystal structure of Streptomyces tyrosinase in a complex with caddie soaked in a Cu(II)-containing solution for 80 hr: occupancy of CuA is low== |
| - | <StructureSection load='3awv' size='340' side='right' caption='[[3awv]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='3awv' size='340' side='right'caption='[[3awv]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3awv]] is a 2 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=3AWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AWV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3awv]] is a 2 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=3AWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AWV 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>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aws|3aws]], [[3awt|3awt]], [[3awu|3awu]], [[3aww|3aww]], [[3awx|3awx]], [[3awy|3awy]], [[3awz|3awz]], [[3ax0|3ax0]]</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>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=3awv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3awv OCA], [https://pdbe.org/3awv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3awv RCSB], [https://www.ebi.ac.uk/pdbsum/3awv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3awv 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>
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| - | <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=3awv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3awv OCA], [http://pdbe.org/3awv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3awv RCSB], [http://www.ebi.ac.uk/pdbsum/3awv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3awv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q83WS2_9ACTN Q83WS2_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Tyrosinase|Tyrosinase]] | + | *[[Tyrosinase 3D structures|Tyrosinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces castaneoglobisporus yen]] | + | [[Category: Large Structures]] |
| - | [[Category: Tyrosinase]] | + | [[Category: Streptomyces castaneoglobisporus]] |
| - | [[Category: Matoba, Y]] | + | [[Category: Matoba Y]] |
| - | [[Category: Sugiyama, M]] | + | [[Category: Sugiyama M]] |
| - | [[Category: Binary complex]]
| + | |
| - | [[Category: Copper transfer]]
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| - | [[Category: Oxidoreductase-metal transport complex]]
| + | |
| - | [[Category: Type-3 copper]]
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| Structural highlights
Function
Q83WS2_9ACTN
Publication Abstract from PubMed
The Cu(II)-soaked crystal structure of tyrosinase that is present in a complex with a protein, designated "caddie," which we previously determined, possesses two copper ions at its catalytic center. We had identified two copper-binding sites in the caddie protein and speculated that copper bound to caddie may be transported to the tyrosinase catalytic center. In our present study, at a 1.16-1.58 A resolution, we determined the crystal structures of tyrosinase complexed with caddie prepared by altering the soaking time of the copper ion and the structures of tyrosinase complexed with different caddie mutants that display little or no capacity to activate tyrosinase. Based on these structures, we propose a molecular mechanism by which two copper ions are transported to the tyrosinase catalytic center with the assistance of caddie acting as a metallochaperone.
A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein.,Matoba Y, Bando N, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M J Biol Chem. 2011 Aug 26;286(34):30219-31. Epub 2011 Jul 5. PMID:21730070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matoba Y, Bando N, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M. A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein. J Biol Chem. 2011 Aug 26;286(34):30219-31. Epub 2011 Jul 5. PMID:21730070 doi:10.1074/jbc.M111.256818
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