1kya

ACTIVE LACCASE FROM TRAMETES VERSICOLOR COMPLEXED WITH 2,5-XYLIDINE

spinqualitylabelsall models 1kya, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1kya is a 4 chain structure with sequence from Trametes versicolor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CU, NAG, PYE, XYD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q96UT7_TRAVE Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laccase 3D structures

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