4hd7: Difference between revisions
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==Crystal Structure of Tyrosinase from Bacillus megaterium V218G mutant soaked in CuSO4== | ==Crystal Structure of Tyrosinase from Bacillus megaterium V218G mutant soaked in CuSO4== | ||
<StructureSection load='4hd7' size='340' side='right' caption='[[4hd7]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4hd7' size='340' side='right' caption='[[4hd7]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hd7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4hd7]] 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=4HD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HD7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hda|4hda]], [[4hd4|4hd4]], [[4hd6|4hd6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hda|4hda]], [[4hd4|4hd4]], [[4hd6|4hd6]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosinase Tyrosinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.18.1 1.14.18.1] </span></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=4hd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hd7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hd7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hd7 PDBsum]</span></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=4hd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hd7 OCA], [http://pdbe.org/4hd7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hd7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hd7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hd7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4hd7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tyrosinase|Tyrosinase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 14581]] | ||
[[Category: | [[Category: Tyrosinase]] | ||
[[Category: Adir, N]] | [[Category: Adir, N]] | ||
[[Category: Fishman, A]] | [[Category: Fishman, A]] | ||
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[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Type 3 copper protein]] | [[Category: Type 3 copper protein]] | ||
Revision as of 11:31, 11 August 2016
Crystal Structure of Tyrosinase from Bacillus megaterium V218G mutant soaked in CuSO4Crystal Structure of Tyrosinase from Bacillus megaterium V218G mutant soaked in CuSO4
Structural highlights
Publication Abstract from PubMedTyrosinase is a type 3 copper enzyme with great potential for production of commercially valuable diphenols from monophenols. However, the use of tyrosinase is limited by its further oxidation of diphenols to quinones. We recently determined the structure of the Bacillus megaterium tyrosinase revealing a residue, V218, which we proposed to take part in positioning of substrates within the active site. In the structure of catechol oxidase from Ipomoea batatas, the lack of monophenolase activity was attributed to the presence of F261 near CuA. Consequently, we engineered two variants, V218F and V218G. V218F was expected to have a decreased monophenolase activity, due to the bulky residue extending into the active site. Surprisingly, both V218F and V218G exhibited a 9- and 4.4-fold higher monophenolase/diphenolase activity ratio, respectively. X-ray structures of variant V218F display a flexibility of the phenylalanine residue along with an adjacent histidine, which we propose to be the source of the change in activity ratio. Influencing the monophenolase/diphenolase activity ratio in tyrosinase.,Goldfeder M, Kanteev M, Adir N, Fishman A Biochim Biophys Acta. 2013 Jan 8. pii: S1570-9639(13)00003-4. doi:, 10.1016/j.bbapap.2012.12.021. PMID:23305929[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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