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1a65

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[[Image:1a65.jpg|left|200px]]
 
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{{Structure
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==TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS==
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|PDB= 1a65 |SIZE=350|CAPTION= <scene name='initialview01'>1a65</scene>, resolution 2.23&Aring;
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<StructureSection load='1a65' size='340' side='right'caption='[[1a65]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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|SITE= <scene name='pdbsite=T1:Type+1+Cu+Binding+Site'>T1</scene> and <scene name='pdbsite=T3:Type+3+Cu+Binding+Site'>T3</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=O:OXYGEN ATOM'>O</scene>
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<table><tr><td colspan='2'>[[1a65]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A65 FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=PYE:TETRAHYDROPYRAN'>PYE</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a65 OCA], [https://pdbe.org/1a65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a65 RCSB], [https://www.ebi.ac.uk/pdbsum/1a65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a65 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9Y780_COPCI Q9Y780_COPCI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a65_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a65 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS'''
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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<ref>PMID:9546223</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1a65" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Laccase 3D structures|Laccase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1A65 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A65 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9546223 9546223]
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[[Category: Coprinopsis cinerea]]
[[Category: Coprinopsis cinerea]]
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[[Category: Laccase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Brzozowski W]]
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[[Category: Brzozowski, W.]]
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[[Category: Ducros V]]
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[[Category: Ducros, V.]]
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[[Category: CU]]
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[[Category: GLC]]
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[[Category: NAG]]
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[[Category: O]]
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[[Category: blue multi-copper oxidase]]
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[[Category: glycoprotein]]
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[[Category: laccase]]
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[[Category: oxidoreductase]]
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[[Category: signal]]
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[[Category: type-2 copper depleted]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:30 2008''
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Current revision

TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS

PDB ID 1a65

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