6zij: Difference between revisions
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==Crystal Structure of Two-Domain Laccase mutant R240H from Streptomyces griseoflavus== | |||
<StructureSection load='6zij' size='340' side='right'caption='[[6zij]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6zij]] 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=6ZIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZIJ 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]] 1.6Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=6zij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zij OCA], [https://pdbe.org/6zij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zij RCSB], [https://www.ebi.ac.uk/pdbsum/6zij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zij ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0M4FJ81_9ACTN A0A0M4FJ81_9ACTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Multi-copper oxidases are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. This process takes place at the trinuclear copper center of the enzymes. Previously, the main catalytic stages for three-domain (3D) laccases have been identified. However, for bacterial small two-domain (2D) laccases several questions remain to be answered. One of them is the nature of the protonation events upon the reductive cleavage of dioxygen to water. In 3D laccases, acidic residues play a key role in the protonation mechanisms. In this study, the role of the Arg240 residue, located within the T2 tunnel of 2D laccase from Streptomyces griseoflavus Ac-993, was investigated. X-ray structural analysis and kinetic characterization of two mutants, R240A and R240H, have provided support for a role of this residue in the protonation events. Communicated by Ramaswamy H. Sarma. | |||
The role of positive charged residue in the proton-transfer mechanism of two-domain laccase from Streptomyces griseoflavus Ac-993.,Gabdulkhakov A, Kolyadenko I, Oliveira P, Tamagnini P, Mikhaylina A, Tishchenko S J Biomol Struct Dyn. 2021 Apr 19:1-8. doi: 10.1080/07391102.2021.1911852. PMID:33870857<ref>PMID:33870857</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6zij" 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 14:52, 1 February 2024
Crystal Structure of Two-Domain Laccase mutant R240H from Streptomyces griseoflavusCrystal Structure of Two-Domain Laccase mutant R240H from Streptomyces griseoflavus
Structural highlights
FunctionPublication Abstract from PubMedMulti-copper oxidases are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. This process takes place at the trinuclear copper center of the enzymes. Previously, the main catalytic stages for three-domain (3D) laccases have been identified. However, for bacterial small two-domain (2D) laccases several questions remain to be answered. One of them is the nature of the protonation events upon the reductive cleavage of dioxygen to water. In 3D laccases, acidic residues play a key role in the protonation mechanisms. In this study, the role of the Arg240 residue, located within the T2 tunnel of 2D laccase from Streptomyces griseoflavus Ac-993, was investigated. X-ray structural analysis and kinetic characterization of two mutants, R240A and R240H, have provided support for a role of this residue in the protonation events. Communicated by Ramaswamy H. Sarma. The role of positive charged residue in the proton-transfer mechanism of two-domain laccase from Streptomyces griseoflavus Ac-993.,Gabdulkhakov A, Kolyadenko I, Oliveira P, Tamagnini P, Mikhaylina A, Tishchenko S J Biomol Struct Dyn. 2021 Apr 19:1-8. doi: 10.1080/07391102.2021.1911852. PMID:33870857[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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