3awv

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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==
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<StructureSection load='3awv' size='340' side='right' caption='[[3awv]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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<StructureSection load='3awv' size='340' side='right'caption='[[3awv]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3awv]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AWV FirstGlance]. <br>
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<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>
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</td></tr><tr><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><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr><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>
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<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>
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<tr><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 Streptomyces castaneoglobisporus]), ORF378 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 Streptomyces castaneoglobisporus])</td></tr>
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<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>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monophenol_monooxygenase Monophenol monooxygenase], 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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</table>
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<tr><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://www.rcsb.org/pdb/explore.do?structureId=3awv RCSB], [http://www.ebi.ac.uk/pdbsum/3awv PDBsum]</span></td></tr>
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== Function ==
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<table>
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[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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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<ref>PMID:21730070</ref>
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<ref>PMID:21730070</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3awv" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Monophenol monooxygenase]]
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[[Category: Large Structures]]
[[Category: Streptomyces castaneoglobisporus]]
[[Category: Streptomyces castaneoglobisporus]]
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[[Category: Matoba, Y.]]
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[[Category: Matoba Y]]
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[[Category: Sugiyama, M.]]
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[[Category: Sugiyama M]]
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[[Category: Binary complex]]
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[[Category: Copper transfer]]
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[[Category: Oxidoreductase-metal transport complex]]
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[[Category: Type-3 copper]]
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[[Category: Tyrosinase]]
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Current revision

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

PDB ID 3awv

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