4j3r: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{STRUCTURE_4j3r|  PDB=4j3r  |  SCENE=  }}
===Crystal structure of catechol oxidase from Aspergillus oryzae, soaked in 4-tert-butylcatechol===
{{ABSTRACT_PUBMED_24043469}}


==About this Structure==
==Crystal structure of catechol oxidase from Aspergillus oryzae, soaked in 4-tert-butylcatechol==
[[4j3r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J3R OCA].  
<StructureSection load='4j3r' size='340' side='right'caption='[[4j3r]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4j3r]] 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=4J3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J3R FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4j3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j3r OCA], [https://pdbe.org/4j3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j3r RCSB], [https://www.ebi.ac.uk/pdbsum/4j3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j3r ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2UNF9_ASPOR Q2UNF9_ASPOR]
<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.


==Reference==
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>
<ref group="xtra">PMID:024043469</ref><references group="xtra"/><references/>
 
[[Category: Catechol oxidase]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Gasparetti, C.]]
</div>
[[Category: Hakulinen, N.]]
<div class="pdbe-citations 4j3r" style="background-color:#fffaf0;"></div>
[[Category: Kaljunen, H.]]
== References ==
[[Category: Rouvinen, J.]]
<references/>
[[Category: Binuclear copper enzyme]]
__TOC__
[[Category: Catechol oxidase]]
</StructureSection>
[[Category: Glycosylated]]
[[Category: Aspergillus oryzae]]
[[Category: Oxidoreductase]]
[[Category: Large Structures]]
[[Category: Type-3 copper center]]
[[Category: Gasparetti C]]
[[Category: Hakulinen N]]
[[Category: Kaljunen H]]
[[Category: Rouvinen J]]

Latest revision as of 15:35, 20 September 2023

Crystal structure of catechol oxidase from Aspergillus oryzae, soaked in 4-tert-butylcatechol

4j3r, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA