title: The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae.
abstract: 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-Å 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 α-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 Å. 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.
authors.affiliation: Department of Chemistry, University of Eastern Finland, Joensuu Campus, PO Box 111, 80101, Joensuu, Finland, nina.hakulinen@uef.fi.
authors.forename: Nina
authors.initials: N
authors.lastname: Hakulinen
authors.forename: Chiara
authors.initials: C
authors.lastname: Gasparetti
authors.forename: Heidi
authors.initials: H
authors.lastname: Kaljunen
authors.forename: Kristiina
authors.initials: K
authors.lastname: Kruus
authors.forename: Juha
authors.initials: J
authors.lastname: Rouvinen
mesh_terms: D000595:Amino Acid Sequence; D001236:Aspergillus oryzae / Q000737:chemistry / Q000201:enzymology*; D020134:Catalytic Domain; D004156:Catechol Oxidase / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D011994:Recombinant Proteins; D010088:Oxidoreductases; D004156:Catechol Oxidase; C412191:monophenolase
references.citation: Phytochemistry. 2012 Sep;81:19-23
references.pmid: 22727580
references.citation: Cell Mol Life Sci. 2005 Aug;62(15):1707-23
references.pmid: 15968468
references.citation: Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55
references.pmid: 15299926
references.citation: Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2240-9
references.pmid: 15572777
references.citation: Protein Sci. 1993 Apr;2(4):597-619
references.pmid: 8518732
references.citation: J Agric Food Chem. 2010 Jan 27;58(2):1189-201
references.pmid: 20039636
references.citation: Phytochemistry. 2006 Nov;67(21):2318-31
references.pmid: 16973188
references.citation: J Mol Biol. 2009 Oct 2;392(4):895-909
references.pmid: 19563811
references.citation: J Biol Chem. 2006 Mar 31;281(13):8981-90
references.pmid: 16436386
references.citation: J Biol Inorg Chem. 2004 Jul;9(5):577-90
references.pmid: 15185133
references.citation: Nat Struct Biol. 1998 Dec;5(12):1084-90
references.pmid: 9846879
references.citation: J Inorg Biochem. 2012 Jun;111:203-9
references.pmid: 22341982
references.citation: Biochemistry. 2011 Jun 21;50(24):5477-86
references.pmid: 21598903
references.citation: J Biol Inorg Chem. 1999 Feb;4(1):56-63
references.pmid: 10499103
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42
references.pmid: 21460441
references.citation: Angew Chem Int Ed Engl. 2006 Jul 10;45(28):4546-50
references.pmid: 16795103
references.citation: J Inorg Biochem. 2006 Jan;100(1):108-23
references.pmid: 16332393
references.citation: Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jun 1;67(Pt 6):672-4
references.pmid: 21636908
references.citation: Int J Mol Sci. 2012;13(7):8398-429
references.pmid: 22942711
references.citation: Curr Opin Struct Biol. 1999 Dec;9(6):677-83
references.pmid: 10607672
references.citation: J Biol Chem. 1974 Jan 25;249(2):335-45
references.pmid: 4358546
references.citation: Biochim Biophys Acta. 1995 Feb 22;1247(1):1-11
references.pmid: 7873577
references.citation: J Biol Inorg Chem. 2003 May;8(5):567-576
references.pmid: 12634912
references.citation: Chem Rev. 2004 Feb;104(2):1013-45
references.pmid: 14871148
references.citation: J Mol Biol. 1998 May 15;278(4):855-70
references.pmid: 9614947
references.citation: J Mol Biol. 2007 Sep 21;372(3):774-97
references.pmid: 17681537
references.citation: J Mol Biol. 2011 Jan 7;405(1):227-37
references.pmid: 21040728
references.citation: Chem Rev. 1996 Nov 7;96(7):2563-2606
references.pmid: 11848837
references.citation: Biochem Biophys Res Commun. 2006 Dec 1;350(4):929-34
references.pmid: 17045575
references.citation: Appl Microbiol Biotechnol. 2010 Mar;86(1):213-26
references.pmid: 19798497
references.citation: Proc Natl Acad Sci U S A. 2008 Jun 17;105(24):8256-61
references.pmid: 18550810
references.citation: Arch Biochem Biophys. 2008 Mar 15;471(2):159-67
references.pmid: 18237542
references.citation: FEBS Lett. 1999 Feb 19;445(1):103-10
references.pmid: 10069382
references.citation: FEBS Lett. 1998 Oct 2;436(2):293-9
references.pmid: 9781698
references.citation: Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
references.pmid: 15572765
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21
references.pmid: 20124702
references.citation: J Inorg Biochem. 2008 Dec;102(12):2160-70
references.pmid: 18829115