5i3b: Difference between revisions
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==Crystal Structure of tyrosinase from Bacillus megaterium with configuration B of hydroquinone inhibitor in the active site== | |||
<StructureSection load='5i3b' size='340' side='right' caption='[[5i3b]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5i3b]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I3B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I3B 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5i3a|5i3a]]</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=5i3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i3b OCA], [http://pdbe.org/5i3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i3b RCSB], [http://www.ebi.ac.uk/pdbsum/5i3b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i3b 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5i3b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Adir, N]] | [[Category: Adir, N]] | ||
[[Category: Deri, B]] | |||
[[Category: Fishman, A]] | [[Category: Fishman, A]] | ||
[[Category: | [[Category: Kanteev, M]] | ||
[[Category: Di-copper oxidase]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 12:34, 19 October 2016
Crystal Structure of tyrosinase from Bacillus megaterium with configuration B of hydroquinone inhibitor in the active siteCrystal Structure of tyrosinase from Bacillus megaterium with configuration B of hydroquinone inhibitor in the active site
Structural highlights
Publication Abstract from PubMedTyrosinases 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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