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==Crystal Structure of Two-Domain Laccase mutant H165F from Streptomyces griseoflavus with high copper ions occupancy== | ==Crystal Structure of Two-Domain Laccase mutant H165F from Streptomyces griseoflavus with high copper ions occupancy== | ||
<StructureSection load='6fc7' size='340' side='right' caption='[[6fc7]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='6fc7' size='340' side='right'caption='[[6fc7]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fc7]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FC7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6fc7]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_griseoflavus"_krainsky_1914 "actinomyces griseoflavus" krainsky 1914]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FC7 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</scene></td></tr> | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mkm|5mkm]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mkm|5mkm]]</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=6fc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fc7 OCA], [http://pdbe.org/6fc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fc7 RCSB], [http://www.ebi.ac.uk/pdbsum/6fc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fc7 ProSAT]</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=6fc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fc7 OCA], [http://pdbe.org/6fc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fc7 RCSB], [http://www.ebi.ac.uk/pdbsum/6fc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fc7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Laccases (EC 1.10.3.2) are multicopper oxidoreductases acting on diphenols and related substances. Laccases are highly important for biotechnology and environmental remediation. These enzymes contain mononuclear one T2 copper ion and two T3 copper ions (Cu3alpha and Cu3beta), which form the so-called trinuclear center (TNC). Along with the typical three-domain laccases Bacteria produce two-domain (2D) enzymes, which are active at neutral and basic pH, thermostable, and resistant to inhibitors. In this work we present the comparative analysis of crystal structures and catalytic properties of recombinant 2D laccase from Streptomyces griseoflavus Ac-993 (SgfSL) and its four mutant forms with replacements of two amino acid residues, located at the narrowing of the presumable T3-solvent tunnels. We obtained inactive enzymes with substitutions of His165, with Phe, and Ile170 with Ala or Phe. His165Ala variant was more active than the wild type. We suggest that His165 is a "gateway" at the O2-tunnel leading from solvent to the Cu3beta of the enzyme. The side chain of Ile170 could be indirectly involved in the coordination of copper ions at the T3 center by maintaining the position of the imidazole ring of His157 that belongs to the first coordination sphere of Cu3alpha. | |||
Investigations of Accessibility of T2/T3 Copper Center of Two-Domain Laccase from Streptomyces griseoflavus Ac-993.,Gabdulkhakov A, Kolyadenko I, Kostareva O, Mikhaylina A, Oliveira P, Tamagnini P, Lisov A, Tishchenko S Int J Mol Sci. 2019 Jun 28;20(13). pii: ijms20133184. doi: 10.3390/ijms20133184. PMID:31261802<ref>PMID:31261802</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6fc7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Laccase 3D structures|Laccase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Actinomyces griseoflavus krainsky 1914]] | |||
[[Category: Laccase]] | [[Category: Laccase]] | ||
[[Category: Large Structures]] | |||
[[Category: Gabdulkhakov, A G]] | [[Category: Gabdulkhakov, A G]] | ||
[[Category: Tishchenko, T V]] | [[Category: Tishchenko, T V]] | ||
Latest revision as of 15:30, 17 July 2019
Crystal Structure of Two-Domain Laccase mutant H165F from Streptomyces griseoflavus with high copper ions occupancyCrystal Structure of Two-Domain Laccase mutant H165F from Streptomyces griseoflavus with high copper ions occupancy
Structural highlights
Publication Abstract from PubMedLaccases (EC 1.10.3.2) are multicopper oxidoreductases acting on diphenols and related substances. Laccases are highly important for biotechnology and environmental remediation. These enzymes contain mononuclear one T2 copper ion and two T3 copper ions (Cu3alpha and Cu3beta), which form the so-called trinuclear center (TNC). Along with the typical three-domain laccases Bacteria produce two-domain (2D) enzymes, which are active at neutral and basic pH, thermostable, and resistant to inhibitors. In this work we present the comparative analysis of crystal structures and catalytic properties of recombinant 2D laccase from Streptomyces griseoflavus Ac-993 (SgfSL) and its four mutant forms with replacements of two amino acid residues, located at the narrowing of the presumable T3-solvent tunnels. We obtained inactive enzymes with substitutions of His165, with Phe, and Ile170 with Ala or Phe. His165Ala variant was more active than the wild type. We suggest that His165 is a "gateway" at the O2-tunnel leading from solvent to the Cu3beta of the enzyme. The side chain of Ile170 could be indirectly involved in the coordination of copper ions at the T3 center by maintaining the position of the imidazole ring of His157 that belongs to the first coordination sphere of Cu3alpha. Investigations of Accessibility of T2/T3 Copper Center of Two-Domain Laccase from Streptomyces griseoflavus Ac-993.,Gabdulkhakov A, Kolyadenko I, Kostareva O, Mikhaylina A, Oliveira P, Tamagnini P, Lisov A, Tishchenko S Int J Mol Sci. 2019 Jun 28;20(13). pii: ijms20133184. doi: 10.3390/ijms20133184. PMID:31261802[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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