1v10: Difference between revisions
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Revision as of 17:13, 30 October 2007
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STRUCTURE OF RIGIDOPORUS LIGNOSUS LACCASE FROM HEMIHEDRALLY TWINNED CRYSTALS
OverviewOverview
Laccase is a multicopper blue oxidase that couples the four-electron, reduction of oxygen with the oxidation of a broad range of organic, substrates, including phenols and arylamines. The enzyme is the object of, intense biotechnological research, due to its employment in bioremediation, of soils and water as well as in other biotechnological applications. We, report here the cDNA and protein sequences, the post-translational, modifications, the crystallization and X-ray structure determination of a, laccase from the white-rot fungus Rigidoporus lignosus. The amino acid, residues sequence deduced from cDNA clearly identified a pre-sequence of, 21 residues representing the signal for extra-cellular localization. Mass, spectrometry analysis performed on the salvage enzyme, confirmed the, ... [(full description)]
About this StructureAbout this Structure
1V10 is a [Single protein] structure of sequence from [Rigidoporus microporus] with CU as [ligand]. Active as [Laccase], with EC number [1.10.3.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair., Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, Rizzi M, J Mol Biol. 2004 Oct 1;342(5):1519-31. PMID:15364578
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