3ntm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of Tyrosinase from Bacillus megaterium crystallized in the absence of zinc, partial occupancy of CuB== | ==Crystal Structure of Tyrosinase from Bacillus megaterium crystallized in the absence of zinc, partial occupancy of CuB== | ||
<StructureSection load='3ntm' size='340' side='right' caption='[[3ntm]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3ntm' size='340' side='right'caption='[[3ntm]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ntm]] 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=3NTM OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[3ntm]] 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=3NTM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3NTM 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" id="ligandDat"><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]], [[3nq0|3nq0]], [[3nq1|3nq1]], [[3nq5|3nq5]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nm8|3nm8]], [[3npy|3npy]], [[3nq0|3nq0]], [[3nq1|3nq1]], [[3nq5|3nq5]]</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='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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ntm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ntm OCA], [http://pdbe.org/3ntm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ntm RCSB], [http://www.ebi.ac.uk/pdbsum/3ntm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ntm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 20: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Tyrosinase|Tyrosinase]] | *[[Tyrosinase 3D structures|Tyrosinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 26: | Line 26: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 14581]] | [[Category: Atcc 14581]] | ||
[[Category: Large Structures]] | |||
[[Category: Tyrosinase]] | [[Category: Tyrosinase]] | ||
[[Category: Adir, N]] | [[Category: Adir, N]] | ||
Revision as of 11:07, 4 November 2020
Crystal Structure of Tyrosinase from Bacillus megaterium crystallized in the absence of zinc, partial occupancy of CuBCrystal Structure of Tyrosinase from Bacillus megaterium crystallized in the absence of zinc, partial occupancy of CuB
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
|
| ||||||||||||||||||||