View source for 6jua


==Aspergillus oryzae pro-tyrosinase oxygen-bound C92A mutant==
<StructureSection load='6jua' size='340' side='right'caption='[[6jua]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jua]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JUA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</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=PER:PEROXIDE+ION'>PER</scene></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=6jua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jua OCA], [https://pdbe.org/6jua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jua RCSB], [https://www.ebi.ac.uk/pdbsum/6jua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jua ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1S9DK56_ASPOZ A0A1S9DK56_ASPOZ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The dinuclear copper enzyme tyrosinase activates O2 to form a (mu-eta2:eta2-peroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate. We herein report the near atomic resolution X-ray crystal structures of the active tyrosinases with substrate L-tyrosine. At their catalytic sites, CuA moved largely toward L-tyrosine (CuA1 to CuA2), whose phenol oxygen directly coordinates to CuA2, involving the movement of CuB (CuB1 to CuB2). The crystal structures and spectroscopic analyses of the dioxygen-bound tyrosinases demonstrated that the peroxide ligand rotated, spontaneously weakening its O-O bond. Thus, the copper migration induced by the substrate-binding accompanied rearrangement of the bound peroxide species so as to facilitate one of the peroxide oxygen atoms to access to the phenol substrate's epsilon carbon atom.

Copper-oxygen Dynamics in Tyrosinase Mechanism.,Fujieda N, Umakoshi K, Ochi Y, Nishikawa Y, Yanagisawa S, Kubo M, Kurisu G, Itoh S Angew Chem Int Ed Engl. 2020 Apr 30. doi: 10.1002/anie.202004733. PMID:32356371<ref>PMID:32356371</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jua" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus oryzae]]
[[Category: Large Structures]]
[[Category: Fujieda N]]
[[Category: Itoh S]]
[[Category: Kurisu G]]
[[Category: Nishikawa Y]]
[[Category: Umakoshi K]]