6rhq: Difference between revisions
New page: '''Unreleased structure''' The entry 6rhq is ON HOLD Authors: Gabdulkhakov, A.G., Tishchenko, T.V., Kolyadenko, I.A. Description: Crystal Structure of Two-Domain Laccase mutant I170A f... |
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==Crystal Structure of Two-Domain Laccase mutant I170A from Streptomyces griseoflavus== | |||
<StructureSection load='6rhq' size='340' side='right'caption='[[6rhq]], [[Resolution|resolution]] 1.98Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rhq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseoflavus Streptomyces griseoflavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RHQ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6rhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rhq OCA], [https://pdbe.org/6rhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rhq RCSB], [https://www.ebi.ac.uk/pdbsum/6rhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rhq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0M4FJ81_9ACTN A0A0M4FJ81_9ACTN] | |||
<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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6rhq" style="background-color:#fffaf0;"></div> | ||
[[Category: Gabdulkhakov | |||
[[Category: Kolyadenko | ==See Also== | ||
*[[Laccase 3D structures|Laccase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces griseoflavus]] | |||
[[Category: Gabdulkhakov AG]] | |||
[[Category: Kolyadenko IA]] | |||
[[Category: Tishchenko TV]] | |||
Latest revision as of 15:20, 24 January 2024
Crystal Structure of Two-Domain Laccase mutant I170A from Streptomyces griseoflavusCrystal Structure of Two-Domain Laccase mutant I170A from Streptomyces griseoflavus
Structural highlights
FunctionPublication 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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