4p6t: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4p6t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P6T FirstGlance]. <br> | <table><tr><td colspan='2'>[[4p6t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P6T FirstGlance]. <br> | ||
</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=YRL:4-(2-HYDROXYETHYL)PHENOL'>YRL</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]] 2.5Å</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=YRL:4-(2-HYDROXYETHYL)PHENOL'>YRL</scene></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=4p6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6t OCA], [https://pdbe.org/4p6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p6t RCSB], [https://www.ebi.ac.uk/pdbsum/4p6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p6t ProSAT]</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=4p6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6t OCA], [https://pdbe.org/4p6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p6t RCSB], [https://www.ebi.ac.uk/pdbsum/4p6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p6t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 03:40, 28 December 2023
Crystal Structure of tyrosinase from Bacillus megaterium with p-tyrosol in the active siteCrystal Structure of tyrosinase from Bacillus megaterium with p-tyrosol in the active site
Structural highlights
FunctionPublication Abstract from PubMedTyrosinase is responsible for the two initial enzymatic steps in the conversion of tyrosine to melanin. Many tyrosinase mutations are the leading cause of albinism in humans, and it is a prominent biotechnology and pharmaceutical industry target. Here we present crystal structures that show that both monophenol hydroxylation and diphenol oxidation occur at the same site. It is suggested that concurrent presence of a phenylalanine above the active site and a restricting thioether bond on the histidine coordinating CuA prevent hydroxylation of monophenols by catechol oxidases. Furthermore, a conserved water molecule activated by E195 and N205 is proposed to mediate deprotonation of the monophenol at the active site. Overall, the structures reveal precise steps in the enzymatic catalytic cycle as well as differences between tyrosinases and other type-3 copper enzymes. Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins.,Goldfeder M, Kanteev M, Isaschar-Ovdat S, Adir N, Fishman A Nat Commun. 2014 Jul 30;5:4505. doi: 10.1038/ncomms5505. PMID:25074014[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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