2zwf - Revision history

OCA at 13:58, 1 November 2023

OCA — Wed, 01 Nov 2023 13:58:41 GMT

←Older revision		Revision as of 13:58, 1 November 2023
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	<StructureSection load='2zwf' size='340' side='right'caption='[[2zwf]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='2zwf' size='340' side='right'caption='[[2zwf]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zwf]] is a 2 chain structure with sequence from [https://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=2ZWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZWF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zwf]] 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=2ZWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZWF FirstGlance]. <br>
-	</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>	+	</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='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~DAH~~:~~3,4-DIHYDROXYPHENYLALANINE~~'>~~DAH~~</scene><~~/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=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;~~'>~~[[1wxc\|1wxc]], [[1wx2\|1wx2]], [[2zmx\|2zmx]], [[2zmy\|2zmy]], [[2zmz\|2zmz]], [[2zwc\|2zwc]], [[2zwd\|2zwd]], [[2zwe\|2zwe]], [[2zwg\|2zwg]]~~</~~div~~>~~</td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TYRC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 "Actinomyces castaneoglobisporus" Yen]), ~~ORF378 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 "Actinomyces castaneoglobisporus" Yen])~~<~~/td></tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Tyrosinase Tyrosinase], with EC number [https://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=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [https://pdbe.org/2zwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [https://www.ebi.ac.uk/pdbsum/2zwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zwf ProSAT]</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=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [https://pdbe.org/2zwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [https://www.ebi.ac.uk/pdbsum/2zwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zwf 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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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zwf ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zwf ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== 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<ref>PMID:16436386</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2zwf" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Tyrosinase 3D structures\|Tyrosinase 3D structures]]		*[[Tyrosinase 3D structures\|Tyrosinase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Actinomyces castaneoglobisporus yen]]
	[[Category: Large Structures]]		[[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]]~~	+
-	~~[[Category: Dioxygen]]~~	+
-	~~[[Category: Oxidoreductase-metal transport complex]]~~	+
-	~~[[Category: Type-3 copper~~]]	+

OCA at 17:39, 15 December 2021

OCA — Wed, 15 Dec 2021 17:39:28 GMT

←Older revision		Revision as of 17:39, 15 December 2021
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	==Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes==		==Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes==
-	<StructureSection load='2zwf' size='340' side='right' caption='[[2zwf]], [[Resolution\|resolution]] 1.40Å' scene=''>	+	<StructureSection load='2zwf' size='340' side='right'caption='[[2zwf]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zwf]] 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=2ZWF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ZWF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zwf]] is a 2 chain structure with sequence from [https://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=2ZWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZWF 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='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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1wxc\|1wxc]], [[1wx2\|1wx2]], [[2zmx\|2zmx]], [[2zmy\|2zmy]], [[2zmz\|2zmz]], [[2zwc\|2zwc]], [[2zwd\|2zwd]], [[2zwe\|2zwe]], [[2zwg\|2zwg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wxc\|1wxc]], [[1wx2\|1wx2]], [[2zmx\|2zmx]], [[2zmy\|2zmy]], [[2zmz\|2zmz]], [[2zwc\|2zwc]], [[2zwd\|2zwd]], [[2zwe\|2zwe]], [[2zwg\|2zwg]]</div></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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TYRC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 "Actinomyces castaneoglobisporus" Yen]), ORF378 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 "Actinomyces castaneoglobisporus" Yen])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tyrosinase Tyrosinase], with EC number [https://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~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [~~http~~://pdbe.org/2zwf PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2zwf PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2zwf ProSAT]</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=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [https://pdbe.org/2zwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [https://www.ebi.ac.uk/pdbsum/2zwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zwf ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	==See Also==		==See Also==
-	*[[Tyrosinase\|Tyrosinase]]	+	*[[Tyrosinase 3D structures\|Tyrosinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Actinomyces castaneoglobisporus yen]]		[[Category: Actinomyces castaneoglobisporus yen]]
		+	[[Category: Large Structures]]
	[[Category: Tyrosinase]]		[[Category: Tyrosinase]]
	[[Category: Matoba, Y]]		[[Category: Matoba, Y]]

OCA at 07:18, 18 October 2018

OCA — Thu, 18 Oct 2018 07:18:10 GMT

←Older revision		Revision as of 07:18, 18 October 2018
Line 1:		Line 1:
		+
	==Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes==		==Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes==
	<StructureSection load='2zwf' size='340' side='right' caption='[[2zwf]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='2zwf' size='340' side='right' caption='[[2zwf]], [[Resolution\|resolution]] 1.40Å' scene=''>
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	<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='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='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='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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [http://pdbe.org/2zwf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [http://www.ebi.ac.uk/pdbsum/2zwf PDBsum]</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=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [http://pdbe.org/2zwf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [http://www.ebi.ac.uk/pdbsum/2zwf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zwf ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zw/2zwf_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zw/2zwf_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 05:03, 7 February 2016

OCA — Sun, 07 Feb 2016 05:03:58 GMT

←Older revision		Revision as of 05:03, 7 February 2016
Line 7:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1wxc\|1wxc]], [[1wx2\|1wx2]], [[2zmx\|2zmx]], [[2zmy\|2zmy]], [[2zmz\|2zmz]], [[2zwc\|2zwc]], [[2zwd\|2zwd]], [[2zwe\|2zwe]], [[2zwg\|2zwg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1wxc\|1wxc]], [[1wx2\|1wx2]], [[2zmx\|2zmx]], [[2zmy\|2zmy]], [[2zmz\|2zmz]], [[2zwc\|2zwc]], [[2zwd\|2zwd]], [[2zwe\|2zwe]], [[2zwg\|2zwg]]</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='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='activity'><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>	+	<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [http://www.ebi.ac.uk/pdbsum/2zwf PDBsum]</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=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [http://pdbe.org/2zwf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [http://www.ebi.ac.uk/pdbsum/2zwf PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zwf ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2zwf" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Actinomyces castaneoglobisporus yen]]		[[Category: Actinomyces castaneoglobisporus yen]]
-	[[Category: ~~Monophenol monooxygenase~~]]	+	[[Category: Tyrosinase]]
	[[Category: Matoba, Y]]		[[Category: Matoba, Y]]
	[[Category: Sugiyama, M]]		[[Category: Sugiyama, M]]
Line 44:		Line 45:
	[[Category: Oxidoreductase-metal transport complex]]		[[Category: Oxidoreductase-metal transport complex]]
	[[Category: Type-3 copper]]		[[Category: Type-3 copper]]
-	[[Category: Tyrosinase]]

OCA at 09:30, 20 January 2015

OCA — Tue, 20 Jan 2015 09:30:14 GMT

←Older revision		Revision as of 09:30, 20 January 2015
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+
		+	==See Also==
		+	*[[Tyrosinase\|Tyrosinase]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	[[Category: Actinomyces castaneoglobisporus yen]]		[[Category: Actinomyces castaneoglobisporus yen]]
	[[Category: Monophenol monooxygenase]]		[[Category: Monophenol monooxygenase]]
-	[[Category: Matoba, Y.]]	+	[[Category: Matoba, Y]]
-	[[Category: Sugiyama, M.]]	+	[[Category: Sugiyama, M]]
	[[Category: Binary complex]]		[[Category: Binary complex]]
	[[Category: Copper transfer]]		[[Category: Copper transfer]]

OCA at 06:40, 10 October 2014

OCA — Fri, 10 Oct 2014 06:40:33 GMT

OCA at 11:05, 14 May 2014

OCA — Wed, 14 May 2014 11:05:00 GMT

←Older revision		Revision as of 11:05, 14 May 2014
Line 1:		Line 1:
-	[[~~Image:~~2zwf.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes==
		+	<StructureSection load='2zwf' size='340' side='right' caption='[[2zwf]], [[Resolution\|resolution]] 1.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2zwf]] 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=2ZWF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZWF FirstGlance]. <br>
		+	</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>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1wxc\|1wxc]], [[1wx2\|1wx2]], [[2zmx\|2zmx]], [[2zmy\|2zmy]], [[2zmz\|2zmz]], [[2zwc\|2zwc]], [[2zwd\|2zwd]], [[2zwe\|2zwe]], [[2zwg\|2zwg]]</td></tr>
		+	<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 "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><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>
		+	<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=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [http://www.ebi.ac.uk/pdbsum/2zwf PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zw/2zwf_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== 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<ref>PMID:16436386</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2zwf"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_2zwf\| PDB=2zwf \| SCENE= }}~~	+

-	~~===Crystal structure~~ of the ~~copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_16436386}}, adds the Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 16436386 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+	[[Category: Actinomyces castaneoglobisporus yen]]
-	~~{{ABSTRACT_PUBMED_16436386}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2zwf]] 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=2ZWF OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:016436386<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Monophenol monooxygenase]]		[[Category: Monophenol monooxygenase]]
-	[[Category: Streptomyces castaneoglobisporus]]
	[[Category: Matoba, Y.]]		[[Category: Matoba, Y.]]
	[[Category: Sugiyama, M.]]		[[Category: Sugiyama, M.]]

OCA: Protected "2zwf" [edit=sysop:move=sysop]

OCA — Wed, 31 Aug 2011 05:53:25 GMT

Protected "2zwf" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:53, 31 August 2011

OCA at 05:53, 31 August 2011

OCA — Wed, 31 Aug 2011 05:53:23 GMT

←Older revision		Revision as of 05:53, 31 August 2011
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:2zwf.png\|left\|200px]]
-	[[Image:2zwf.~~jpg~~\|left\|200px]]	+

	<!--		<!--
Line 12:		Line 11:
	===Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes===		===Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_16436386}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 16436386 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_16436386}}

	==About this Structure==		==About this Structure==
-	~~2ZWF~~ is a 2 ~~chains~~ structure ~~of sequences~~ 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=2ZWF OCA].	+	[[2zwf]] 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=2ZWF OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16436386~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016436386</ref><references group="xtra"/>
	[[Category: Monophenol monooxygenase]]		[[Category: Monophenol monooxygenase]]
	[[Category: Streptomyces castaneoglobisporus]]		[[Category: Streptomyces castaneoglobisporus]]
Line 25:		Line 30:
	[[Category: Copper transfer]]		[[Category: Copper transfer]]
	[[Category: Dioxygen]]		[[Category: Dioxygen]]
-	[[Category: Oxidoreductase/metal transport complex]]	+	[[Category: Oxidoreductase-metal transport complex]]
	[[Category: Type-3 copper]]		[[Category: Type-3 copper]]
	[[Category: Tyrosinase]]		[[Category: Tyrosinase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 16 13:41:12 2009''

OCA at 11:41, 16 December 2009

OCA — Wed, 16 Dec 2009 11:41:14 GMT

←Older revision		Revision as of 11:41, 16 December 2009
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:2zwf.jpg\|left\|200px]]

-	The ~~entry 2zwf~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_2zwf", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_2zwf\| PDB=2zwf \| SCENE= }}

-	~~Authors: Matoba, Y., Sugiyama, M.~~	+	===Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes===

-	Description: Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 80 minutes

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Sep 3 15~~:15:08 2009''	+	==About this Structure==
		+	2ZWF is a 2 chains structure of sequences 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=2ZWF OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:16436386</ref><references group="xtra"/>
		+	[[Category: Monophenol monooxygenase]]
		+	[[Category: Streptomyces castaneoglobisporus]]
		+	[[Category: Matoba, Y.]]
		+	[[Category: Sugiyama, M.]]
		+	[[Category: Binary complex]]
		+	[[Category: Copper transfer]]
		+	[[Category: Dioxygen]]
		+	[[Category: Oxidoreductase/metal transport complex]]
		+	[[Category: Type-3 copper]]
		+	[[Category: Tyrosinase]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 16 13:41:12 2009''

←Older revision		Revision as of 06:40, 10 October 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2zwf]] 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=2ZWF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZWF FirstGlance]. <br>		<table><tr><td colspan='2'>[[2zwf]] 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=2ZWF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZWF FirstGlance]. <br>
-	</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>	+	</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>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1wxc\|1wxc]], [[1wx2\|1wx2]], [[2zmx\|2zmx]], [[2zmy\|2zmy]], [[2zmz\|2zmz]], [[2zwc\|2zwc]], [[2zwd\|2zwd]], [[2zwe\|2zwe]], [[2zwg\|2zwg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1wxc\|1wxc]], [[1wx2\|1wx2]], [[2zmx\|2zmx]], [[2zmy\|2zmy]], [[2zmz\|2zmz]], [[2zwc\|2zwc]], [[2zwd\|2zwd]], [[2zwe\|2zwe]], [[2zwg\|2zwg]]</td></tr>
-	<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 "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='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><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>	+	<tr id='activity'><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>
-	<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=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [http://www.ebi.ac.uk/pdbsum/2zwf PDBsum]</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=2zwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zwf RCSB], [http://www.ebi.ac.uk/pdbsum/2zwf PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 26:		Line 26:
	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<ref>PMID:16436386</ref>		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<ref>PMID:16436386</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==