1a65

From Proteopedia

Revision as of 12:40, 30 October 2007

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, ... [(full description)]

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

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