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]] 1.89&Aring;' scene=''>
+<StructureSection load='4jhu' size='340' side='right'caption='[[4jhu]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4jhu]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JHU FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jhv|4jhv]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jhu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jhu RCSB], [http://www.ebi.ac.uk/pdbsum/4jhu PDBsum]</span></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&reg;/PubMed&reg;, 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: Fedorova, T V]]
+[[Category: Large Structures]]
-[[Category: Glazunova, O A]]
+[[Category: Fedorova TV]]
-[[Category: Koroleva, O A]]
+[[Category: Glazunova OA]]
-[[Category: Kurzeev, S A]]
+[[Category: Koroleva OA]]
-[[Category: Maloshenok, L G]]
+[[Category: Kurzeev SA]]
-[[Category: Polyakov, K M]]
+[[Category: Maloshenok LG]]
-[[Category: 4-copper protein]]
+[[Category: Polyakov KM]]
-[[Category: Beta sheet]]
-[[Category: Laccase]]
-[[Category: Metal-binding]]
-[[Category: Oxidoreductase]]