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==Aspergillus oryzae active-tyrosinase copper-depleted C92A mutant== | ==Aspergillus oryzae active-tyrosinase copper-depleted C92A mutant== | ||
<StructureSection load='6ju6' size='340' side='right'caption='[[6ju6]]' scene=''> | <StructureSection load='6ju6' size='340' side='right'caption='[[6ju6]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JU6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JU6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ju6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspoz Aspoz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JU6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JU6 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ju6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ju6 OCA], [http://pdbe.org/6ju6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ju6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ju6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ju6 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OAory_01107480 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5062 ASPOZ])</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://proteopedia.org/fgij/fg.htm?mol=6ju6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ju6 OCA], [http://pdbe.org/6ju6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ju6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ju6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ju6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ju6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aspoz]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fujieda N]] | [[Category: Tyrosinase]] | ||
[[Category: Itoh S]] | [[Category: Fujieda, N]] | ||
[[Category: Kurisu G]] | [[Category: Itoh, S]] | ||
[[Category: Nishikawa Y]] | [[Category: Kurisu, G]] | ||
[[Category: Umakoshi K]] | [[Category: Nishikawa, Y]] | ||
[[Category: Umakoshi, K]] | |||
[[Category: Copper enzyme]] | |||
[[Category: Dinuclear copper center]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 12:55, 12 August 2020
Aspergillus oryzae active-tyrosinase copper-depleted C92A mutantAspergillus oryzae active-tyrosinase copper-depleted C92A mutant
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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