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[[Image:1v10.gif|left|200px]]


{{Structure
==Structure of Rigidoporus lignosus laccase from hemihedrally twinned crystals==
|PDB= 1v10 |SIZE=350|CAPTION= <scene name='initialview01'>1v10</scene>, resolution 1.7&Aring;
<StructureSection load='1v10' size='340' side='right'caption='[[1v10]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+A'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>
<table><tr><td colspan='2'>[[1v10]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rigidoporus_microporus Rigidoporus microporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V10 FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=  
<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></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v10 OCA], [https://pdbe.org/1v10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v10 RCSB], [https://www.ebi.ac.uk/pdbsum/1v10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v10 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v10 OCA], [http://www.ebi.ac.uk/pdbsum/1v10 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v10 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/Q6H9H7_9APHY Q6H9H7_9APHY]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/1v10_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1v10 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Laccase is a multicopper blue oxidase that couples the four-electron reduction of oxygen with the oxidation of a broad range of organic substrates, including phenols and arylamines. The enzyme is the object of intense biotechnological research, due to its employment in bioremediation of soils and water as well as in other biotechnological applications. We report here the cDNA and protein sequences, the post-translational modifications, the crystallization and X-ray structure determination of a laccase from the white-rot fungus Rigidoporus lignosus. The amino acid residues sequence deduced from cDNA clearly identified a pre-sequence of 21 residues representing the signal for extra-cellular localization. Mass spectrometry analysis performed on the salvage enzyme, confirmed the deduced sequence and precisely mapped two glycosylation sites at Asn337 and Asn435, determining the nature of the bound glycosidic moieties. The crystal structure was determined at 1.7A resolution from perfectly hemihedrally twinned crystals, by molecular replacement technique. While the overall structure closely resembled those reported for other fungal laccases, the analysis of the T2/T3 trinuclear cluster revealed an unprecedented coordination sphere for the T3 copper pair. No bridging oxygen ligand was present between the two T3 copper ions, which were no longer symmetrically coordinated. The observed structure could represent an intermediate along the process of four-electron reduction of oxygen to water taking place at the trinuclear copper cluster.


'''STRUCTURE OF RIGIDOPORUS LIGNOSUS LACCASE FROM HEMIHEDRALLY TWINNED CRYSTALS'''
The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair.,Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, Rizzi M J Mol Biol. 2004 Oct 1;342(5):1519-31. PMID:15364578<ref>PMID:15364578</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1v10" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Laccase is a multicopper blue oxidase that couples the four-electron reduction of oxygen with the oxidation of a broad range of organic substrates, including phenols and arylamines. The enzyme is the object of intense biotechnological research, due to its employment in bioremediation of soils and water as well as in other biotechnological applications. We report here the cDNA and protein sequences, the post-translational modifications, the crystallization and X-ray structure determination of a laccase from the white-rot fungus Rigidoporus lignosus. The amino acid residues sequence deduced from cDNA clearly identified a pre-sequence of 21 residues representing the signal for extra-cellular localization. Mass spectrometry analysis performed on the salvage enzyme, confirmed the deduced sequence and precisely mapped two glycosylation sites at Asn337 and Asn435, determining the nature of the bound glycosidic moieties. The crystal structure was determined at 1.7A resolution from perfectly hemihedrally twinned crystals, by molecular replacement technique. While the overall structure closely resembled those reported for other fungal laccases, the analysis of the T2/T3 trinuclear cluster revealed an unprecedented coordination sphere for the T3 copper pair. No bridging oxygen ligand was present between the two T3 copper ions, which were no longer symmetrically coordinated. The observed structure could represent an intermediate along the process of four-electron reduction of oxygen to water taking place at the trinuclear copper cluster.
*[[Laccase 3D structures|Laccase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1V10 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rigidoporus_microporus Rigidoporus microporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V10 OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair., Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, Rizzi M, J Mol Biol. 2004 Oct 1;342(5):1519-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15364578 15364578]
[[Category: Laccase]]
[[Category: Rigidoporus microporus]]
[[Category: Rigidoporus microporus]]
[[Category: Single protein]]
[[Category: Cambria A]]
[[Category: Cambria, A.]]
[[Category: Garavaglia S]]
[[Category: Garavaglia, S.]]
[[Category: Palmieri F]]
[[Category: Palmieri, F.]]
[[Category: Rizzi M]]
[[Category: Rizzi, M.]]
[[Category: multicopper blue oxidase]]
[[Category: oxidase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:18:05 2008''

Latest revision as of 07:57, 17 October 2024

Structure of Rigidoporus lignosus laccase from hemihedrally twinned crystalsStructure of Rigidoporus lignosus laccase from hemihedrally twinned crystals

Structural highlights

1v10 is a 1 chain structure with sequence from Rigidoporus microporus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6H9H7_9APHY

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Laccase is a multicopper blue oxidase that couples the four-electron reduction of oxygen with the oxidation of a broad range of organic substrates, including phenols and arylamines. The enzyme is the object of intense biotechnological research, due to its employment in bioremediation of soils and water as well as in other biotechnological applications. We report here the cDNA and protein sequences, the post-translational modifications, the crystallization and X-ray structure determination of a laccase from the white-rot fungus Rigidoporus lignosus. The amino acid residues sequence deduced from cDNA clearly identified a pre-sequence of 21 residues representing the signal for extra-cellular localization. Mass spectrometry analysis performed on the salvage enzyme, confirmed the deduced sequence and precisely mapped two glycosylation sites at Asn337 and Asn435, determining the nature of the bound glycosidic moieties. The crystal structure was determined at 1.7A resolution from perfectly hemihedrally twinned crystals, by molecular replacement technique. While the overall structure closely resembled those reported for other fungal laccases, the analysis of the T2/T3 trinuclear cluster revealed an unprecedented coordination sphere for the T3 copper pair. No bridging oxygen ligand was present between the two T3 copper ions, which were no longer symmetrically coordinated. The observed structure could represent an intermediate along the process of four-electron reduction of oxygen to water taking place at the trinuclear copper cluster.

The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair.,Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, Rizzi M J Mol Biol. 2004 Oct 1;342(5):1519-31. PMID:15364578[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, Rizzi M. The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair. J Mol Biol. 2004 Oct 1;342(5):1519-31. PMID:15364578 doi:10.1016/j.jmb.2004.07.100

1v10, resolution 1.70Å

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