4oua
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Coexistent single-crystal structure of latent and active mushroom tyrosinase (abPPO4) mediated by a hexatungstotellurate(VI)== |
| + | <StructureSection load='4oua' size='340' side='right' caption='[[4oua]], [[Resolution|resolution]] 2.76Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4oua]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OUA FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TEW:6-TUNGSTOTELLURATE(VI)'>TEW</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene></td></tr> | ||
| + | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oua OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oua RCSB], [http://www.ebi.ac.uk/pdbsum/4oua PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tyrosinase exhibits catalytic activity for the ortho-hydroxylation of monophenols to diphenols as well as their subsequent oxidation to quinones. Owing to polymerization of these quinones, brown-coloured high-molecular-weight compounds called melanins are generated. The latent precursor form of polyphenol oxidase 4, one of the six tyrosinase isoforms from Agaricus bisporus, was purified to homogeneity and crystallized. The obtained crystals belonged to space group C121 (two molecules per asymmetric unit) and diffracted to 2.78 A resolution. The protein only formed crystals under low-salt conditions using the 6-tungstotellurate(VI) salt Na6[TeW6O24] . 22H2O as a co-crystallization agent. | ||
| - | + | Crystallization and preliminary X-ray crystallographic analysis of latent isoform PPO4 mushroom (Agaricus bisporus) tyrosinase.,Mauracher SG, Molitor C, Al-Oweini R, Kortz U, Rompel A Acta Crystallogr F Struct Biol Commun. 2014 Feb;70(Pt 2):263-6. doi:, 10.1107/S2053230X14000582. Epub 2014 Jan 23. PMID:24637771<ref>PMID:24637771</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Agaricus bisporus]] | ||
| + | [[Category: Tyrosinase]] | ||
| + | [[Category: Al-Oweini, R.]] | ||
| + | [[Category: Kortz, U.]] | ||
| + | [[Category: Mauracher, St G.]] | ||
| + | [[Category: Molitor, C.]] | ||
| + | [[Category: Rompel, A.]] | ||
| + | [[Category: Anderson-evans-type polyoxometalate]] | ||
| + | [[Category: Hetero-protein co-crystallization]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Ppo4]] | ||
| + | [[Category: Type-3 copper protein]] | ||
| + | [[Category: Tyrosinase]] | ||
| + | [[Category: Tyrosinase maturation]] | ||
| + | [[Category: Zymogen]] | ||
Revision as of 06:25, 25 June 2014
Coexistent single-crystal structure of latent and active mushroom tyrosinase (abPPO4) mediated by a hexatungstotellurate(VI)
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