1a65
From Proteopedia
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|PDB= 1a65 |SIZE=350|CAPTION= <scene name='initialview01'>1a65</scene>, resolution 2.23Å | |PDB= 1a65 |SIZE=350|CAPTION= <scene name='initialview01'>1a65</scene>, resolution 2.23Å | ||
|SITE= <scene name='pdbsite=T1:Type+1+Cu+Binding+Site'>T1</scene> and <scene name='pdbsite=T3:Type+3+Cu+Binding+Site'>T3</scene> | |SITE= <scene name='pdbsite=T1:Type+1+Cu+Binding+Site'>T1</scene> and <scene name='pdbsite=T3:Type+3+Cu+Binding+Site'>T3</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a65 OCA], [http://www.ebi.ac.uk/pdbsum/1a65 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a65 RCSB]</span> | ||
}} | }} | ||
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[[Category: Brzozowski, W.]] | [[Category: Brzozowski, W.]] | ||
[[Category: Ducros, V.]] | [[Category: Ducros, V.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: GLC]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: O]] | ||
[[Category: blue multi-copper oxidase]] | [[Category: blue multi-copper oxidase]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: type-2 copper depleted]] | [[Category: type-2 copper depleted]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:08 2008'' |
Revision as of 15:34, 30 March 2008
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| , resolution 2.23Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , , | ||||||
| Activity: | Laccase, with EC number 1.10.3.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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