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| | <StructureSection load='3dkh' size='340' side='right'caption='[[3dkh]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3dkh' size='340' side='right'caption='[[3dkh]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dkh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_16460 Atcc 16460]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DKH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dkh]] 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=3DKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DKH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gw0|1gw0]], [[2ih8|2ih8]], [[2ih9|2ih9]], [[2q9o|2q9o]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LAC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204285 ATCC 16460])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Laccase Laccase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dkh OCA], [https://pdbe.org/3dkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dkh RCSB], [https://www.ebi.ac.uk/pdbsum/3dkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dkh ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dkh OCA], [https://pdbe.org/3dkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dkh RCSB], [https://www.ebi.ac.uk/pdbsum/3dkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dkh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LAC1_MELAO LAC1_MELAO]] Lignin degradation and detoxification of lignin-derived products (Probable).<ref>PMID:15474046</ref>
| + | [https://www.uniprot.org/uniprot/LAC1_MELAO LAC1_MELAO] Lignin degradation and detoxification of lignin-derived products (Probable).<ref>PMID:15474046</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 16460]] | |
| - | [[Category: Laccase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hakulinen, N]] | + | [[Category: Melanocarpus albomyces]] |
| - | [[Category: Rouvinen, J]] | + | [[Category: Hakulinen N]] |
| - | [[Category: Ascomycete]] | + | [[Category: Rouvinen J]] |
| - | [[Category: C-terminal mutant]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Lignin degradation]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Multicopper oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
3dkh is a 2 chain structure with sequence from Melanocarpus albomyces. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.4Å |
| Ligands: | , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
LAC1_MELAO Lignin degradation and detoxification of lignin-derived products (Probable).[1]
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
The C-terminus of the fungal laccase from Melanocarpus albomyces (MaL) is processed during secretion at a processing site conserved among the ascomycete laccases. The three-dimensional structure of MaL has been solved as one of the first complete laccase structures. According to the crystal structure of MaL, the four C-terminal amino acids of the mature protein penetrate into a tunnel leading towards the trinuclear site. The C-terminal carboxylate group forms a hydrogen bond with a side chain of His140, which also coordinates to the type 3 copper. In order to analyze the role of the processed C-terminus, site-directed mutagenesis of the MaL cDNA was performed, and the mutated proteins were expressed in Trichoderma reesei and Saccharomyces cerevisiae. Changes in the C-terminus of MaL caused major defects in protein production in both expression hosts. The deletion of the last four amino acids dramatically affected the activity of the enzyme, as the deletion mutant delDSGL(559) was practically inactive. Detailed characterization of the purified L559A mutant expressed in S. cerevisiae showed the importance of the C-terminal plug for laccase activity, stability, and kinetics. Moreover, the crystal structure of the L559A mutant expressed in S. cerevisiae showed that the C-terminal mutation had clearly affected the trinuclear site geometry. The results in this study clearly confirm the critical role of the last amino acids in the C-terminus of MaL.
Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure.,Andberg M, Hakulinen N, Auer S, Saloheimo M, Koivula A, Rouvinen J, Kruus K FEBS J. 2009 Nov;276(21):6285-300. Epub 2009 Sep 24. PMID:19780817[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kiiskinen LL, Palonen H, Linder M, Viikari L, Kruus K. Laccase from Melanocarpus albomyces binds effectively to cellulose. FEBS Lett. 2004 Oct 8;576(1-2):251-5. PMID:15474046 doi:S0014579304010440
- ↑ Andberg M, Hakulinen N, Auer S, Saloheimo M, Koivula A, Rouvinen J, Kruus K. Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure. FEBS J. 2009 Nov;276(21):6285-300. Epub 2009 Sep 24. PMID:19780817 doi:10.1111/j.1742-4658.2009.07336.x
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