3v9e: Difference between revisions
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[[ | ==Structure of the L513M mutant of the laccase from B.aclada== | ||
<StructureSection load='3v9e' size='340' side='right' caption='[[3v9e]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v9e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Botrytis_aclada Botrytis aclada]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V9E FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sqr|3sqr]]</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=3v9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v9e RCSB], [http://www.ebi.ac.uk/pdbsum/3v9e PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Laccases are members of a large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. These enzymes contain four Cu atoms per molecule organized into three sites: T1, T2 and T3. In all laccases, the T1 copper ion is coordinated by two histidines and one cysteine in the equatorial plane and is covered by the side chains of hydrophobic residues in the axial positions. The redox potential of the T1 copper ion influences the enzymatic reaction and is determined by the nature of the axial ligands and the structure of the second coordination sphere. In this work, the laccase from the ascomycete Botrytis aclada was studied, which contains conserved Ile491 and nonconserved Leu499 residues in the axial positions. The three-dimensional structures of the wild-type enzyme and the L499M mutant were determined by X-ray crystallography at 1.7 A resolution. Crystals suitable for X-ray analysis could only be grown after deglycosylation. Both structures did not contain the T2 copper ion. The catalytic properties of the enzyme were characterized and the redox potentials of both enzyme forms were determined: E0 = 720 and 580 mV for the wild-type enzyme and the mutant, respectively. Since the structures of the wild-type and mutant forms are very similar, the change in the redox potential can be related to the L499M mutation in the T1 site of the enzyme. | |||
Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties.,Osipov E, Polyakov K, Kittl R, Shleev S, Dorovatovsky P, Tikhonova T, Hann S, Ludwig R, Popov V Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):2913-23. doi:, 10.1107/S1399004714020380. Epub 2014 Oct 23. PMID:25372682<ref>PMID:25372682</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Botrytis aclada]] | [[Category: Botrytis aclada]] | ||
[[Category: Laccase]] | [[Category: Laccase]] | ||
[[Category: Dorovatovsky, P V | [[Category: Dorovatovsky, P V]] | ||
[[Category: Kittl, R | [[Category: Kittl, R]] | ||
[[Category: Ludwig, R | [[Category: Ludwig, R]] | ||
[[Category: Osipov, E M | [[Category: Osipov, E M]] | ||
[[Category: Polyakov, K M | [[Category: Polyakov, K M]] | ||
[[Category: Popov, V O | [[Category: Popov, V O]] | ||
[[Category: Shleev, S V | [[Category: Shleev, S V]] | ||
[[Category: Tikhonova, T V | [[Category: Tikhonova, T V]] | ||
[[Category: Glycosylation]] | [[Category: Glycosylation]] | ||
[[Category: Multicopper oxidase]] | [[Category: Multicopper oxidase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 13:47, 19 November 2014
Structure of the L513M mutant of the laccase from B.acladaStructure of the L513M mutant of the laccase from B.aclada
Structural highlights
Publication Abstract from PubMedLaccases are members of a large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. These enzymes contain four Cu atoms per molecule organized into three sites: T1, T2 and T3. In all laccases, the T1 copper ion is coordinated by two histidines and one cysteine in the equatorial plane and is covered by the side chains of hydrophobic residues in the axial positions. The redox potential of the T1 copper ion influences the enzymatic reaction and is determined by the nature of the axial ligands and the structure of the second coordination sphere. In this work, the laccase from the ascomycete Botrytis aclada was studied, which contains conserved Ile491 and nonconserved Leu499 residues in the axial positions. The three-dimensional structures of the wild-type enzyme and the L499M mutant were determined by X-ray crystallography at 1.7 A resolution. Crystals suitable for X-ray analysis could only be grown after deglycosylation. Both structures did not contain the T2 copper ion. The catalytic properties of the enzyme were characterized and the redox potentials of both enzyme forms were determined: E0 = 720 and 580 mV for the wild-type enzyme and the mutant, respectively. Since the structures of the wild-type and mutant forms are very similar, the change in the redox potential can be related to the L499M mutation in the T1 site of the enzyme. Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties.,Osipov E, Polyakov K, Kittl R, Shleev S, Dorovatovsky P, Tikhonova T, Hann S, Ludwig R, Popov V Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):2913-23. doi:, 10.1107/S1399004714020380. Epub 2014 Oct 23. PMID:25372682[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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