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4j3q
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of truncated catechol oxidase from Aspergillus oryzae== | |
| - | === | + | <StructureSection load='4j3q' size='340' side='right' caption='[[4j3q]], [[Resolution|resolution]] 2.90Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4j3q]] 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=4J3Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J3Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j3p|4j3p]], [[4j3r|4j3r]]</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=4j3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j3q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j3q RCSB], [http://www.ebi.ac.uk/pdbsum/4j3q PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24043469</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspoz]] | ||
[[Category: Catechol oxidase]] | [[Category: Catechol oxidase]] | ||
| - | [[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: Binuclear copper enzyme]] | ||
| - | [[Category: Catechol oxidase]] | ||
[[Category: Glycosylated]] | [[Category: Glycosylated]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Type-3 copper center]] | [[Category: Type-3 copper center]] | ||
Revision as of 17:05, 21 December 2014
Crystal structure of truncated catechol oxidase from Aspergillus oryzae
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