4jhu: Difference between revisions
No edit summary |
No edit summary |
||
Line 7: | Line 7: | ||
<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'>[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> | ||
</table> | </table> | ||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |