6ju8: Difference between revisions
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<StructureSection load='6ju8' size='340' side='right'caption='[[6ju8]], [[Resolution|resolution]] 1.27Å' scene=''> | <StructureSection load='6ju8' size='340' side='right'caption='[[6ju8]], [[Resolution|resolution]] 1.27Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ju8]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6ju8]] 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=6JU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JU8 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.27Å</td></tr> | ||
<tr id=' | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ju8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ju8 OCA], [https://pdbe.org/6ju8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ju8 RCSB], [https://www.ebi.ac.uk/pdbsum/6ju8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ju8 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1S9DK56_ASPOZ A0A1S9DK56_ASPOZ] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 6ju8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6ju8" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aspergillus oryzae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fujieda N]] | |||
[[Category: Fujieda | [[Category: Itoh S]] | ||
[[Category: Itoh | [[Category: Kurisu G]] | ||
[[Category: Kurisu | [[Category: Nishikawa Y]] | ||
[[Category: Nishikawa | [[Category: Umakoshi K]] | ||
[[Category: Umakoshi | |||
Latest revision as of 13:19, 22 November 2023
Aspergillus oryzae active-tyrosinase copper-bound C92A mutantAspergillus oryzae active-tyrosinase copper-bound C92A mutant
Structural highlights
FunctionPublication 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. See AlsoReferences
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