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| | ==Crystal structure of laccase from Cerrena maxima at 1.9A resolution== | | ==Crystal structure of laccase from Cerrena maxima at 1.9A resolution== |
| - | <StructureSection load='2h5u' size='340' side='right' caption='[[2h5u]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='2h5u' size='340' side='right'caption='[[2h5u]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2h5u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trametes_maxima Trametes maxima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H5U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2h5u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trametes_maxima Trametes maxima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H5U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene></td></tr> | + | <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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kya|1kya]]</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=2h5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5u OCA], [https://pdbe.org/2h5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h5u RCSB], [https://www.ebi.ac.uk/pdbsum/2h5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h5u ProSAT]</span></td></tr> |
| - | <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>
| + | |
| - | <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=2h5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h5u RCSB], [http://www.ebi.ac.uk/pdbsum/2h5u PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LAC1_TRAMX LAC1_TRAMX] Lignin degradation and detoxification of lignin-derived products.<ref>PMID:16944230</ref> <ref>PMID:17012782</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/2h5u_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/2h5u_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | + | </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=2h5u ConSurf]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2h5u" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Laccase 3D structures|Laccase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Laccase]] | + | [[Category: Large Structures]] |
| | [[Category: Trametes maxima]] | | [[Category: Trametes maxima]] |
| - | [[Category: Bento, I]] | + | [[Category: Bento I]] |
| - | [[Category: Betzel, C]] | + | [[Category: Betzel C]] |
| - | [[Category: Gabdoulkhakov, A G]] | + | [[Category: Gabdoulkhakov AG]] |
| - | [[Category: Lamzin, V S]] | + | [[Category: Lamzin VS]] |
| - | [[Category: Lindley, P F]] | + | [[Category: Lindley PF]] |
| - | [[Category: Lyashenko, A V]] | + | [[Category: Lyashenko AV]] |
| - | [[Category: Mikhailov, A M]] | + | [[Category: Mikhailov AM]] |
| - | [[Category: Zaitsev, V N]] | + | [[Category: Zaitsev VN]] |
| - | [[Category: Zhukhlistova, N E]] | + | [[Category: Zhukhlistova NE]] |
| - | [[Category: Zhukova, Y N]] | + | [[Category: Zhukova YN]] |
| - | [[Category: Blue multi-copper enzyme]]
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| - | [[Category: Crystal]]
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| - | [[Category: Laccase from cerrena maxima]]
| + | |
| - | [[Category: Oxidoreductase]]
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| - | [[Category: Purification]]
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| - | [[Category: X-ray analyse]]
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| Structural highlights
Function
LAC1_TRAMX Lignin degradation and detoxification of lignin-derived products.[1] [2]
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
Laccases are members of the blue multi-copper oxidase family that oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. Crystals of the laccase from Cerrena maxima have been obtained and X-ray data were collected to 1.9 A resolution using synchrotron radiation. A preliminary analysis shows that the enzyme has the typical laccase structure and several carbohydrate sites have been identified. The carbohydrate chains appear to be involved in stabilization of the intermolecular contacts in the crystal structure, thus promoting the formation of well ordered crystals of the enzyme. Here, the results of an X-ray crystallographic study on the laccase from the fungus Cerrena maxima are reported. Crystals that diffract well to a resolution of at least 1.9 A (R factor = 18.953%; R(free) = 23.835; r.m.s.d. bond lengths, 0.06 A; r.m.s.d. bond angles, 1.07 degrees) have been obtained despite the presence of glycan moieties. The overall spatial organization of C. maxima laccase and the structure of its copper-containing active centre have been determined by the molecular-replacement method using the laccase from Trametes versicolor (Piontek et al., 2002) as a structural template. In addition, four glycan-binding sites were identified and the 1.9 A X-ray data were used to determine the previously unknown primary structure of this protein. The identity (calculated from sequence alignment) between the C. maxima laccase and the T. versicolor laccase is about 87%. Tyr196 and Tyr372 show significant extra density at the ortho positions and this has been interpreted in terms of NO(2) substituents.
Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima.,Lyashenko AV, Zhukhlistova NE, Gabdoulkhakov AG, Zhukova YN, Voelter W, Zaitsev VN, Bento I, Stepanova EV, Kachalova GS, Koroleva OV, Cherkashyn EA, Tishkov VI, Lamzin VS, Schirwitz K, Morgunova EY, Betzel C, Lindley PF, Mikhailov AM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):954-7. Epub 2006 Sep 19. PMID:17012782[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lyashenko AV, Bento I, Zaitsev VN, Zhukhlistova NE, Zhukova YN, Gabdoulkhakov AG, Morgunova EY, Voelter W, Kachalova GS, Stepanova EV, Koroleva OV, Lamzin VS, Tishkov VI, Betzel C, Lindley PF, Mikhailov AM. X-ray structural studies of the fungal laccase from Cerrena maxima. J Biol Inorg Chem. 2006 Nov;11(8):963-73. PMID:16944230 doi:10.1007/s00775-006-0158-x
- ↑ Lyashenko AV, Zhukhlistova NE, Gabdoulkhakov AG, Zhukova YN, Voelter W, Zaitsev VN, Bento I, Stepanova EV, Kachalova GS, Koroleva OV, Cherkashyn EA, Tishkov VI, Lamzin VS, Schirwitz K, Morgunova EY, Betzel C, Lindley PF, Mikhailov AM. Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):954-7. Epub 2006 Sep 19. PMID:17012782 doi:10.1107/S1744309106036578
- ↑ Lyashenko AV, Zhukhlistova NE, Gabdoulkhakov AG, Zhukova YN, Voelter W, Zaitsev VN, Bento I, Stepanova EV, Kachalova GS, Koroleva OV, Cherkashyn EA, Tishkov VI, Lamzin VS, Schirwitz K, Morgunova EY, Betzel C, Lindley PF, Mikhailov AM. Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):954-7. Epub 2006 Sep 19. PMID:17012782 doi:10.1107/S1744309106036578
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