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==Crystal Structure of Tyrosinase from Bacillus megaterium crystallized in the absence of Zinc== | |||
<StructureSection load='3nq0' size='340' side='right' caption='[[3nq0]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3nq0]] 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=3NQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NQ0 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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nm8|3nm8]], [[3npy|3npy]], [[3nq1|3nq1]], [[3nq5|3nq5]], [[3ntm|3ntm]]</td></tr> | |||
<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=3nq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nq0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nq0 RCSB], [http://www.ebi.ac.uk/pdbsum/3nq0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tyrosinase is a member of the type 3 copper enzyme family that is involved in the production of melanin in a wide range of organisms. The crystal structures of a tyrosinase from Bacillus megaterium were determined at a resolution of 2.0-2.3 A. The enzyme crystallized as a dimer in the asymmetric unit and was shown to be active in crystal. The overall monomeric structure is similar to that of the monomer of the previously determined tyrosinase from Streptomyces castaneoglobisporus, but it does not contain an accessory Cu-binding "caddie" protein. Two Cu(II) ions, serving as the major cofactors within the active site, are coordinated by six conserved histidine residues. However, determination of structures under different conditions shows varying occupancies and positions of the copper ions. This apparent mobility in copper binding modes indicates that there is a pathway by which copper is accumulated or lost by the enzyme. Additionally, we suggest that residues R209 and V218, situated in a second shell of residues surrounding the active site, play a role in substrate binding orientation based on their flexibility and position. The determination of a structure with the inhibitor kojic acid, the first tyrosinase structure with a bound ligand, revealed additional residues involved in the positioning of substrates in the active site. Comparison of wild-type structures with the structure of the site-specific variant R209H, which possesses a higher monophenolase/diphenolase activity ratio, lends further support to a previously suggested mechanism by which monophenolic substrates dock mainly to CuA. | |||
First Structures of an Active Bacterial Tyrosinase Reveal Copper Plasticity.,Sendovski M, Kanteev M, Ben-Yosef VS, Adir N, Fishman A J Mol Biol. 2010 Oct 30. PMID:21040728<ref>PMID:21040728</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Journal:JBIC:21|Journal:JBIC:21]] | *[[Journal:JBIC:21|Journal:JBIC:21]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atcc 14581]] | [[Category: Atcc 14581]] | ||
[[Category: Tyrosinase]] | [[Category: Tyrosinase]] | ||
[[Category: Adir, N | [[Category: Adir, N]] | ||
[[Category: Fishman, A | [[Category: Fishman, A]] | ||
[[Category: Kanteev, M | [[Category: Kanteev, M]] | ||
[[Category: Sendovski, M | [[Category: Sendovski, M]] | ||
[[Category: Bacillus megaterium]] | [[Category: Bacillus megaterium]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Type3 copper protein]] | [[Category: Type3 copper protein]] | ||
Revision as of 01:53, 4 January 2015
Crystal Structure of Tyrosinase from Bacillus megaterium crystallized in the absence of ZincCrystal Structure of Tyrosinase from Bacillus megaterium crystallized in the absence of Zinc
Structural highlights
Publication Abstract from PubMedTyrosinase is a member of the type 3 copper enzyme family that is involved in the production of melanin in a wide range of organisms. The crystal structures of a tyrosinase from Bacillus megaterium were determined at a resolution of 2.0-2.3 A. The enzyme crystallized as a dimer in the asymmetric unit and was shown to be active in crystal. The overall monomeric structure is similar to that of the monomer of the previously determined tyrosinase from Streptomyces castaneoglobisporus, but it does not contain an accessory Cu-binding "caddie" protein. Two Cu(II) ions, serving as the major cofactors within the active site, are coordinated by six conserved histidine residues. However, determination of structures under different conditions shows varying occupancies and positions of the copper ions. This apparent mobility in copper binding modes indicates that there is a pathway by which copper is accumulated or lost by the enzyme. Additionally, we suggest that residues R209 and V218, situated in a second shell of residues surrounding the active site, play a role in substrate binding orientation based on their flexibility and position. The determination of a structure with the inhibitor kojic acid, the first tyrosinase structure with a bound ligand, revealed additional residues involved in the positioning of substrates in the active site. Comparison of wild-type structures with the structure of the site-specific variant R209H, which possesses a higher monophenolase/diphenolase activity ratio, lends further support to a previously suggested mechanism by which monophenolic substrates dock mainly to CuA. First Structures of an Active Bacterial Tyrosinase Reveal Copper Plasticity.,Sendovski M, Kanteev M, Ben-Yosef VS, Adir N, Fishman A J Mol Biol. 2010 Oct 30. PMID:21040728[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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