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3qpk

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==Probing oxygen channels in Melanocarpus albomyces laccase==
==Probing oxygen channels in Melanocarpus albomyces laccase==
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<StructureSection load='3qpk' size='340' side='right' caption='[[3qpk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='3qpk' size='340' side='right'caption='[[3qpk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qpk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Melanocarpus_albomyces Melanocarpus albomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QPK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qpk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Melanocarpus_albomyces Melanocarpus albomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
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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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gw0|1gw0]], [[2ih8|2ih8]], [[2ih9|2ih9]], [[2q9o|2q9o]], [[3dkh|3dkh]], [[3fu7|3fu7]], [[3fu8|3fu8]], [[3fu9|3fu9]], [[3pps|3pps]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LAC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204285 Melanocarpus albomyces])</td></tr>
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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=3qpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpk OCA], [https://pdbe.org/3qpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpk RCSB], [https://www.ebi.ac.uk/pdbsum/3qpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpk ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qpk RCSB], [http://www.ebi.ac.uk/pdbsum/3qpk PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/LAC1_MELAO LAC1_MELAO] Lignin degradation and detoxification of lignin-derived products (Probable).<ref>PMID:15474046</ref>
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Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center.
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Probing the Dioxygen Route in Melanocarpus albomyces Laccase with Pressurized Xenon Gas.,Kallio JP, Rouvinen J, Kruus K, Hakulinen N Biochemistry. 2011 May 5. PMID:21524088<ref>PMID:21524088</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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==See Also==
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</div>
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*[[Laccase 3D structures|Laccase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Laccase]]
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[[Category: Large Structures]]
[[Category: Melanocarpus albomyces]]
[[Category: Melanocarpus albomyces]]
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[[Category: Hakulinen, N]]
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[[Category: Hakulinen N]]
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[[Category: Kallio, J P]]
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[[Category: Kallio JP]]
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[[Category: Rouvinen, J]]
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[[Category: Rouvinen J]]
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[[Category: Cu binding]]
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[[Category: Multicopper oxidase]]
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[[Category: Oxidoreductase]]
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[[Category: Xe binding]]
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Current revision

Probing oxygen channels in Melanocarpus albomyces laccase

PDB ID 3qpk

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