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6gsg

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'''Unreleased structure'''
 
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The entry 6gsg is ON HOLD
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==Crystal structure of Aspergillus oryzae catechol oxidase complexed with resorcinol==
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<StructureSection load='6gsg' size='340' side='right'caption='[[6gsg]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6gsg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae_RIB40 Aspergillus oryzae RIB40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GSG FirstGlance]. <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]] 2.192&#8491;</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=RCO:RESORCINOL'>RCO</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=6gsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsg OCA], [https://pdbe.org/6gsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gsg RCSB], [https://www.ebi.ac.uk/pdbsum/6gsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q2UNF9_ASPOR Q2UNF9_ASPOR]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Catechol oxidases and tyrosinases are coupled binuclear copper enzymes that oxidize various o-diphenolic compounds to corresponding o-quinones. Tyrosinases have an additional monooxygenation ability to hydroxylate monophenol to o-diphenol. It is still not clear what causes the difference in the catalytic activities. We solved a complex structure of Aspergillus oryzae catechol oxidase with resorcinol bound into the active site. Catalytic activity of A. oryzae catechol oxidase was studied, for the first time, by high-resolution FT-ICR mass spectrometry to shed light on the reaction mechanism. The enzyme was also found to catalyze monooxygenation of small phenolics, which provides a novel perspective for the discussion of differences in the catalytic activity between tyrosinases and catechol oxidases. According to the results, two binding modes for resorcinol are suggested and a reaction mechanism for coupled binuclear copper enzymes is discussed.
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Authors: Penttinen, L., Hakulinen, N., Rouvinen, J.
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Unraveling substrate specificity and catalytic promiscuity of Aspergillus oryzae catechol oxidase.,Penttinen L, Rutanen C, Janis J, Rouvinen J, Hakulinen N Chembiochem. 2018 Sep 11. doi: 10.1002/cbic.201800387. PMID:30204291<ref>PMID:30204291</ref>
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Description: Crystal structure of Aspergillus oryzae catechol oxidase complexed with resorcinol
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Rouvinen, J]]
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<div class="pdbe-citations 6gsg" style="background-color:#fffaf0;"></div>
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[[Category: Penttinen, L]]
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== References ==
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[[Category: Hakulinen, N]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aspergillus oryzae RIB40]]
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[[Category: Large Structures]]
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[[Category: Hakulinen N]]
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[[Category: Penttinen L]]
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[[Category: Rouvinen J]]

Current revision

Crystal structure of Aspergillus oryzae catechol oxidase complexed with resorcinol

PDB ID 6gsg

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