5o3k: Difference between revisions
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<StructureSection load='5o3k' size='340' side='right'caption='[[5o3k]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5o3k' size='340' side='right'caption='[[5o3k]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5o3k]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5o3k]] is a 12 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=5O3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O3K 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=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=O:OXYGEN+ATOM'>O</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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5o3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o3k OCA], [https://pdbe.org/5o3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o3k RCSB], [https://www.ebi.ac.uk/pdbsum/5o3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o3k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0M4FJ81_9ACTN A0A0M4FJ81_9ACTN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Streptomyces griseoflavus]] | [[Category: Streptomyces griseoflavus]] | ||
[[Category: | [[Category: Gabdulkhakov AG]] | ||
[[Category: Tishchenko TV]] | |||
Latest revision as of 22:06, 29 November 2023
Crystal Structure of mutant M54L/M64L/M96L of Two-Domain Laccase from Streptomyces griseoflavus with 1 mM copper sulfate on growth mediumCrystal Structure of mutant M54L/M64L/M96L of Two-Domain Laccase from Streptomyces griseoflavus with 1 mM copper sulfate on growth medium
Structural highlights
FunctionPublication Abstract from PubMedLaccase belongs to the family of copper-containing oxidases. A study was made of the mechanism that sustains the incorporation of copper ions into the T2/T3 centers of recombinant two-domain laccase Streptomyces griseoflavus Ac-993. The occupancy of the T3 center by copper ions was found to increase with an increasing copper content in the culture medium and after dialysis of the protein preparation against a copper sulfate-containing buffer. The T2 center was filled only when overproducer strain cells were grown at a higher copper concentration in the medium. Two-domain laccases were assumed to possess a channel that serves to deliver copper ions to the T3 center during the formation of the three-dimensional laccase conformation and dialysis of the protein preparation. A narrower channel leads to the T2 center in two-domain laccases compared with three-domain ones, rendering the center less accessible for copper atoms. The incorporation of copper ions into the T2 center of two-domain laccases is likely to occur in the course of their biosynthesis or the formation of a functional trimer. [Incorporation of Copper Ions into T2/T3 Centers of Two-Domain Laccases].,Gabdulkhakov AG, Kostareva OS, Kolyadenko IA, Mikhaylina AO, Trubitsina LI, Tishchenko SV Mol Biol (Mosk). 2018 Jan-Feb;52(1):29-35. doi: 10.7868/S0026898418010056. PMID:29512633[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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