4j6t: Difference between revisions
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<StructureSection load='4j6t' size='340' side='right'caption='[[4j6t]], [[Resolution|resolution]] 2.43Å' scene=''> | <StructureSection load='4j6t' size='340' side='right'caption='[[4j6t]], [[Resolution|resolution]] 2.43Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4j6t]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4j6t]] 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=4J6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J6T FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.43Å</td></tr> | ||
<tr id=' | <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></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=4j6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j6t OCA], [https://pdbe.org/4j6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j6t RCSB], [https://www.ebi.ac.uk/pdbsum/4j6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j6t ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B2ZB02_PRIMG B2ZB02_PRIMG] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Tyrosinase|Tyrosinase]] | *[[Tyrosinase|Tyrosinase]] | ||
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Priestia megaterium]] | ||
[[Category: Adir | [[Category: Adir N]] | ||
[[Category: Fishman | [[Category: Fishman A]] | ||
[[Category: Goldfeder | [[Category: Goldfeder M]] | ||
[[Category: Kanteev | [[Category: Kanteev M]] | ||
Latest revision as of 18:37, 20 September 2023
Crystal Structure of Tyrosinase from Bacillus megaterium F197A mutantCrystal Structure of Tyrosinase from Bacillus megaterium F197A mutant
Structural highlights
FunctionPublication Abstract from PubMedTyrosinase belongs to the type 3 copper enzyme family, containing a dinuclear copper center, CuA and CuB. It is mainly responsible for melanin production in a wide range of organisms. Although copper ions are essential for the activity of tyrosinase, the mechanism of copper uptake is still unclear. We have recently determined the crystal structure of tyrosinase from Bacillus megaterium (TyrBm) and revealed that this enzyme has tighter binding of CuA in comparison with CuB. Investigating copper accumulation in TyrBm, we found that the presence of copper has a more significant effect on the diphenolase activity. By decreasing the concentration of copper, we increased the diphenolase to monophenolase activity ratio twofold. Using a rational design approach, we identified five variants having an impact on copper uptake. We have found that a major role of the highly conserved Asn205 residue is to stabilize the orientation of the His204 imidazole ring in the binding site, thereby promoting the correct coordination of CuB. Further investigation of these variants revealed that Phe197, Met61, and Met184, which are located at the entrance to the binding site, not only play a role in copper uptake, but are also important for enhancing the diphenolase activity. We propose a mechanism of copper accumulation by the enzyme as well as an approach to changing the selectivity of TyrBm towards L-dopa production. The mechanism of copper uptake by tyrosinase from Bacillus megaterium.,Kanteev M, Goldfeder M, Chojnacki M, Adir N, Fishman A J Biol Inorg Chem. 2013 Dec;18(8):895-903. doi: 10.1007/s00775-013-1034-0. Epub, 2013 Sep 6. PMID:24061559[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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