5i3a: Difference between revisions

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-'''Unreleased structure'''
-The entry 5i3a is ON HOLD  until Paper Publication
+==Crystal Structure of tyrosinase from Bacillus megaterium with configuration A of hydroquinone inhibitor in the active site==
+<StructureSection load='5i3a' size='340' side='right' caption='[[5i3a]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5i3a]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I3A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I3A FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HQE:BENZENE-1,4-DIOL'>HQE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5i3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i3a OCA], [http://pdbe.org/5i3a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i3a RCSB], [http://www.ebi.ac.uk/pdbsum/5i3a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i3a ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Tyrosinases are responsible for melanin formation in all life domains. Tyrosinase inhibitors are used for the prevention of severe skin diseases, in skin-whitening creams and to avoid fruit browning, however continued use of many such inhibitors is considered unsafe. In this study we provide conclusive evidence of the inhibition mechanism of two well studied tyrosinase inhibitors, KA (kojic acid) and HQ (hydroquinone), which are extensively used in hyperpigmentation treatment. KA is reported in the literature with contradicting inhibition mechanisms, while HQ is described as both a tyrosinase inhibitor and a substrate. By visualization of KA and HQ in the active site of TyrBm crystals, together with molecular modeling, binding constant analysis and kinetic experiments, we have elucidated their mechanisms of inhibition, which was ambiguous for both inhibitors. We confirm that while KA acts as a mixed inhibitor, HQ can act both as a TyrBm substrate and as an inhibitor.
-Authors: Kanteev, M., Deri, B., Adir, N., Fishman, A.
+The unravelling of the complex pattern of tyrosinase inhibition.,Deri B, Kanteev M, Goldfeder M, Lecina D, Guallar V, Adir N, Fishman A Sci Rep. 2016 Oct 11;6:34993. doi: 10.1038/srep34993. PMID:27725765<ref>PMID:27725765</ref>
-Description: Crystal Structure of tyrosinase from Bacillus megaterium with configuration A of hydroquinone inhibitor in the active site
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Kanteev, M]]
+<div class="pdbe-citations 5i3a" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Adir, N]]
+[[Category: Deri, B]]
 [[Category: Fishman, A]]
-[[Category: Deri, B]]
+[[Category: Kanteev, M]]
+[[Category: Di-copper oxidase]]
+[[Category: Oxidoreductase]]