1a65
From Proteopedia
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TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS
Overview
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.
About this Structure
1A65 is a Single protein structure of sequence from Coprinopsis cinerea with NAG, GLC, CU and O as ligands. Active as Laccase, with EC number 1.10.3.2 Structure known Active Sites: T1 and T3. Full crystallographic information is available from OCA.
Reference
Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution., Ducros V, Brzozowski AM, Wilson KS, Brown SH, Ostergaard P, Schneider P, Yaver DS, Pedersen AH, Davies GJ, Nat Struct Biol. 1998 Apr;5(4):310-6. PMID:9546223
Page seeded by OCA on Mon Nov 5 12:48:04 2007
Categories: Coprinopsis cinerea | Laccase | Single protein | Brzozowski, W. | Ducros, V. | CU | GLC | NAG | O | Blue multi-copper oxidase | Glycoprotein | Oxidoreductase | Signal | Type-2 copper depleted
