1kya
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(New page: 200px<br /><applet load="1kya" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kya, resolution 2.40Å" /> '''ACTIVE LACCASE FROM ...)
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Revision as of 00:03, 25 November 2007
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ACTIVE LACCASE FROM TRAMETES VERSICOLOR COMPLEXED WITH 2,5-XYLIDINE
Overview
Laccases are multicopper oxidases that catalyze the oxidation of a wide, range of phenols or arylamines, and their use in industrial oxidative, processes is increasing. We purified from the white rot fungus Trametes, versicolor a laccase that exists as five different isozymes, depending on, glycosylation. The 2.4 A resolution structure of the most abundant isozyme, of the glycosylated enzyme was solved. The four copper atoms are present, and it is the first crystal structure of a laccase in its active form. The, crystallized enzyme binds 2,5-xylidine, which was used as a laccase, inducer in the fungus culture. This arylamine is a very weak reducing, substrate of the enzyme. The cavity enclosing 2,5-xylidine is rather wide, allowing the accommodation of substrates of various sizes. Several amino, acid residues make hydrophobic interactions with the aromatic ring of the, ligand. In addition, two charged or polar residues interact with its amino, group. The first one is an histidine that also coordinates the copper that, functions as the primary electron acceptor. The second is an aspartate, conserved among fungal laccases. The purified enzyme can oxidize various, hydroxylated compounds of the phenylurea family of herbicides that we, synthesized. These phenolic substrates have better affinities at pH 5 than, at pH 3, which could be related to the 2,5-xylidine binding by the, aspartate. This is the first high-resolution structure of a multicopper, oxidase complexed to a reducing substrate. It provides a model for, engineering laccases that are either more efficient or with a wider, substrate specificity.
About this Structure
1KYA is a Single protein structure of sequence from Trametes versicolor with NAG, CU, PYE and XYD as ligands. Active as Laccase, with EC number 1.10.3.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics., Bertrand T, Jolivalt C, Briozzo P, Caminade E, Joly N, Madzak C, Mougin C, Biochemistry. 2002 Jun 11;41(23):7325-33. PMID:12044164
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Categories: Laccase | Single protein | Trametes versicolor | Bertrand, T. | Briozzo, P. | Caminade, E. | Jolivalt, C. | Joly, N. | Madzak, C. | Mougin, C. | CU | NAG | PYE | XYD | Blue-copper | Oxidoreductase
