5i3a: Difference between revisions
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==Crystal Structure of tyrosinase from Bacillus megaterium with configuration A of hydroquinone inhibitor in the active site== | ==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]] 2.20Å' scene=''> | <StructureSection load='5i3a' size='340' side='right'caption='[[5i3a]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == 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:// | <table><tr><td colspan='2'>[[5i3a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. 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://proteopedia.org/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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5i3a" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5i3a" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 14581]] | |||
[[Category: Large Structures]] | |||
[[Category: Adir, N]] | [[Category: Adir, N]] | ||
[[Category: Deri, B]] | [[Category: Deri, B]] | ||
Revision as of 11:43, 27 May 2020
Crystal Structure of tyrosinase from Bacillus megaterium with configuration A of hydroquinone inhibitor in the active siteCrystal Structure of tyrosinase from Bacillus megaterium with configuration A 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. See AlsoReferences
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