http://purl.uniprot.org/citations/9546223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9546223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9546223 | http://www.w3.org/2000/01/rdf-schema#comment | "Laccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water. It is widely believed to be the simplest representative of the ubiquitous blue multi-copper oxidase family. Laccase is implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. The structure of laccase from the fungus Coprinus cinereus has been determined by X-ray crystallography at a resolution of 2.2 A. Laccase is a monomer composed of three cupredoxin-like beta-sandwich domains, similar to that found in ascorbate oxidase. In contrast to ascorbate oxidase, however, the mononuclear type-1 Cu site lacks the axial methionine ligand and so exhibits trigonal planar coordination, consistent with its elevated redox potential. Crucially, the structure is trapped in a Cu depleted form in which the putative type-2 Cu atom is completely absent, but in which the remaining type-1 and type-3 Cu sites display full occupancy. Type-2 Cu depletion has unexpected consequences for the coordination of the remaining type-3 Cu atoms."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsb0498-310"xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsb0498-310"xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Davies G.J."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Davies G.J."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Wilson K.S."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Wilson K.S."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Schneider P."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Schneider P."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Brzozowski A.M."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Brzozowski A.M."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Yaver D.S."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Yaver D.S."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Brown S.H."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Brown S.H."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Ducros V."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Ducros V."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Ostergaard P."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Ostergaard P."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Pedersen A.H."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/author | "Pedersen A.H."xsd:string |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9546223 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |