4p6s

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==Crystal Structure of tyrosinase from Bacillus megaterium with L-DOPA in the active site==
==Crystal Structure of tyrosinase from Bacillus megaterium with L-DOPA in the active site==
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<StructureSection load='4p6s' size='340' side='right' caption='[[4p6s]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='4p6s' size='340' side='right'caption='[[4p6s]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4p6s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P6S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4p6s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P6S FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p6r|4p6r]], [[4p6t|4p6t]]</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=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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/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'>[https://proteopedia.org/fgij/fg.htm?mol=4p6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6s OCA], [https://pdbe.org/4p6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p6s RCSB], [https://www.ebi.ac.uk/pdbsum/4p6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p6s ProSAT]</span></td></tr>
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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=4p6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p6s RCSB], [http://www.ebi.ac.uk/pdbsum/4p6s PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/B2ZB02_PRIMG B2ZB02_PRIMG]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tyrosinase is responsible for the two initial enzymatic steps in the conversion of tyrosine to melanin. Many tyrosinase mutations are the leading cause of albinism in humans, and it is a prominent biotechnology and pharmaceutical industry target. Here we present crystal structures that show that both monophenol hydroxylation and diphenol oxidation occur at the same site. It is suggested that concurrent presence of a phenylalanine above the active site and a restricting thioether bond on the histidine coordinating CuA prevent hydroxylation of monophenols by catechol oxidases. Furthermore, a conserved water molecule activated by E195 and N205 is proposed to mediate deprotonation of the monophenol at the active site. Overall, the structures reveal precise steps in the enzymatic catalytic cycle as well as differences between tyrosinases and other type-3 copper enzymes.
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Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins.,Goldfeder M, Kanteev M, Isaschar-Ovdat S, Adir N, Fishman A Nat Commun. 2014 Jul 30;5:4505. doi: 10.1038/ncomms5505. PMID:25074014<ref>PMID:25074014</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4p6s" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Tyrosinase]]
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[[Category: Large Structures]]
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[[Category: Adir, N.]]
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[[Category: Priestia megaterium]]
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[[Category: Fishman, A.]]
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[[Category: Adir N]]
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[[Category: Goldfeder, M.]]
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[[Category: Fishman A]]
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[[Category: Kanteev, M.]]
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[[Category: Goldfeder M]]
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[[Category: L-dopa]]
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[[Category: Kanteev M]]
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[[Category: Oxidoreductase]]
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[[Category: Type 3 copper protein]]
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Crystal Structure of tyrosinase from Bacillus megaterium with L-DOPA in the active site

PDB ID 4p6s

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