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| | ==Crystal structure of full-length catechol oxidase from Aspergillus oryzae== | | ==Crystal structure of full-length catechol oxidase from Aspergillus oryzae== |
| - | <StructureSection load='4j3p' size='340' side='right' caption='[[4j3p]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4j3p' size='340' side='right'caption='[[4j3p]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j3p]] is a 1 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=4J3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J3P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j3p]] is a 1 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=4J3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J3P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><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=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j3q|4j3q]], [[4j3r|4j3r]]</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=4j3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j3p OCA], [https://pdbe.org/4j3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j3p RCSB], [https://www.ebi.ac.uk/pdbsum/4j3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j3p ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5990879 ([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/Catechol_oxidase Catechol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.1 1.10.3.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j3p OCA], [http://pdbe.org/4j3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j3p RCSB], [http://www.ebi.ac.uk/pdbsum/4j3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j3p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2UNF9_ASPOR Q2UNF9_ASPOR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspoz]] | + | [[Category: Aspergillus oryzae]] |
| - | [[Category: Catechol oxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Gasparetti, C]] | + | [[Category: Gasparetti C]] |
| - | [[Category: Hakulinen, N]] | + | [[Category: Hakulinen N]] |
| - | [[Category: Kaljunen, H]] | + | [[Category: Kaljunen H]] |
| - | [[Category: Rouvinen, J]] | + | [[Category: Rouvinen J]] |
| - | [[Category: Binuclear copper enzyme]]
| + | |
| - | [[Category: Glycosylated]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Type-3 copper center]]
| + | |
| Structural highlights
4j3p is a 1 chain structure with sequence from Aspergillus oryzae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q2UNF9_ASPOR
Publication Abstract from PubMed
Catechol oxidases (EC 1.10.3.1) catalyse the oxidation of o-diphenols to their corresponding o-quinones. These oxidases contain two copper ions (CuA and CuB) within the so-called coupled type 3 copper site as found in tyrosinases (EC 1.14.18.1) and haemocyanins. The crystal structures of a limited number of bacterial and fungal tyrosinases and plant catechol oxidases have been solved. In this study, we present the first crystal structure of a fungal catechol oxidase from Aspergillus oryzae (AoCO4) at 2.5-A resolution. AoCO4 belongs to the newly discovered family of short-tyrosinases, which are distinct from other tyrosinases and catechol oxidases because of their lack of the conserved C-terminal domain and differences in the histidine pattern for CuA. The sequence identity of AoCO4 with other structurally known enzymes is low (less than 30 %), and the crystal structure of AoCO4 diverges from that of enzymes belonging to the conventional tyrosinase family in several ways, particularly around the central alpha-helical core region. A diatomic oxygen moiety was identified as a bridging molecule between the two copper ions CuA and CuB separated by a distance of 4.2-4.3 A. The UV/vis absorption spectrum of AoCO4 exhibits a distinct maximum of absorbance at 350 nm, which has been reported to be typical of the oxy form of type 3 copper enzymes.
The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae.,Hakulinen N, Gasparetti C, Kaljunen H, Kruus K, Rouvinen J J Biol Inorg Chem. 2013 Sep 17. PMID:24043469[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hakulinen N, Gasparetti C, Kaljunen H, Kruus K, Rouvinen J. The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae. J Biol Inorg Chem. 2013 Sep 17. PMID:24043469 doi:10.1007/s00775-013-1038-9
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