1A65
TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS
Summary for 1A65
Entry DOI | 10.2210/pdb1a65/pdb |
Descriptor | LACCASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, TETRAHYDROPYRAN, ... (6 entities in total) |
Functional Keywords | laccase, blue multi-copper oxidase, type-2 copper depleted, oxidoreductase, glycoprotein |
Biological source | Coprinopsis cinerea |
Total number of polymer chains | 1 |
Total formula weight | 55079.42 |
Authors | Ducros, V.,Brzozowski, W. (deposition date: 1998-03-05, release date: 1999-03-30, Last modification date: 2024-12-25) |
Primary citation | Ducros, V.,Brzozowski, A.M.,Wilson, K.S.,Brown, S.H.,Ostergaard, P.,Schneider, P.,Yaver, D.S.,Pedersen, A.H.,Davies, G.J. Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution. Nat.Struct.Biol., 5:310-316, 1998 Cited by PubMed Abstract: 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. PubMed: 9546223DOI: 10.1038/nsb0498-310 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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