4jhu: Difference between revisions
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==T2-depleted laccase from Coriolopsis caperata soaked with CuCl== | |||
<StructureSection load='4jhu' size='340' side='right'caption='[[4jhu]], [[Resolution|resolution]] 1.89Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jhu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coriolopsis_caperata Coriolopsis caperata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JHU 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]] 1.89Å</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=4jhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jhu OCA], [https://pdbe.org/4jhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jhu RCSB], [https://www.ebi.ac.uk/pdbsum/4jhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jhu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/M1GME7_9APHY M1GME7_9APHY] | |||
<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. A new laccase was isolated from the basidiomycete Coriolopsis caperata strain 0677 and its amino-acid sequence was determined. According to its physicochemical properties and spectroscopic features, the laccase from C. caperata is a high redox-potential blue laccase. Attempts to crystallize the native enzyme were unsuccessful. The copper type 2-depleted (T2D) laccase was prepared and crystallized. The structure of T2D laccase from C. caperata was solved at 1.6 A resolution, and attempts to reconstruct the T2 copper centre were performed using Cu(+) and Cu(2+) ions. The structure of T2D+Cu(+) laccase was solved at 1.89 A resolution. It was shown that the T2D+Cu(+) laccase structure contained four copper ions in the active site. Reconstruction could not be achieved when the T2D laccase crystals were treated with CuSO4. | |||
Elucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions.,Glazunova OA, Polyakov KM, Fedorova TV, Dorovatovskii PV, Koroleva OV Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):854-61. doi:, 10.1107/S1399004715001595. Epub 2015 Mar 26. PMID:25849396<ref>PMID:25849396</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4jhu" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Laccase 3D structures|Laccase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Coriolopsis caperata]] | |||
[[Category: Large Structures]] | |||
[[Category: Fedorova TV]] | |||
[[Category: Glazunova OA]] | |||
[[Category: Koroleva OA]] | |||
[[Category: Kurzeev SA]] | |||
[[Category: Maloshenok LG]] | |||
[[Category: Polyakov KM]] | |||