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| - | [[Image:1kya.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1kya| PDB=1kya | SCENE= }} | | {{STRUCTURE_1kya| PDB=1kya | SCENE= }} |
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| - | '''ACTIVE LACCASE FROM TRAMETES VERSICOLOR COMPLEXED WITH 2,5-XYLIDINE'''
| + | ===ACTIVE LACCASE FROM TRAMETES VERSICOLOR COMPLEXED WITH 2,5-XYLIDINE=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12044164}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12044164 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12044164}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Blue-copper]] | | [[Category: Blue-copper]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:19:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:17:16 2008'' |
Revision as of 08:17, 2 July 2008
Template:STRUCTURE 1kya
ACTIVE LACCASE FROM TRAMETES VERSICOLOR COMPLEXED WITH 2,5-XYLIDINE
Template:ABSTRACT PUBMED 12044164
About this Structure
1KYA is a Single protein structure of sequence from Trametes versicolor. 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
Page seeded by OCA on Wed Jul 2 11:17:16 2008
