4oua

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==Coexistent single-crystal structure of latent and active mushroom tyrosinase (abPPO4) mediated by a hexatungstotellurate(VI)==
==Coexistent single-crystal structure of latent and active mushroom tyrosinase (abPPO4) mediated by a hexatungstotellurate(VI)==
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<StructureSection load='4oua' size='340' side='right' caption='[[4oua]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
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<StructureSection load='4oua' size='340' side='right'caption='[[4oua]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[4oua]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agaricus_bisporus_var._bisporus_H97 Agaricus bisporus var. bisporus H97]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4OUA FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.763&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4oua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oua OCA], [https://pdbe.org/4oua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oua RCSB], [https://www.ebi.ac.uk/pdbsum/4oua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oua ProSAT]</span></td></tr>
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<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>
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</table>
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<table>
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<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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.
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Tyrosinases, bifunctional metalloenzymes, catalyze the oxidation of monophenols and o-diphenols to o-quinones, the precursor compounds of the brown-coloured pigment melanin. In eukaryotic organisms, tyrosinases are expressed as latent zymogens that have to be proteolytically cleaved in order to form highly active enzymes. This activation mechanism, known as the tyrosinase maturation process, has scientific and industrial significance with respect to biochemical and technical applications of the enzyme. Here, not only the first crystal structure of the mushroom tyrosinase abPPO4 is presented in its active form (Ser2-Ser383) and in its 21 kDa heavier latent form (Ser2-Thr545), but furthermore the simultaneous presence of both forms within one single-crystal structure is shown. This allows for a simple approach to investigate the transition between these two forms. Isoform abPPO4 was isolated and extensively purified from the natural source (Agaricus bisporus), which contains a total of six polyphenol oxidases (PPOs). The enzyme formed crystals (diffracting to a resolution of 2.76 A) owing to the employment of the 6-tungstotellurate(VI) salt (Na6[TeW6O24].22H2O) as a cocrystallization agent. Two of these disc-shaped Anderson-type polyoxoanions [TeW6O24](6-) separate two asymmetric units comprising one crystallographic heterodimer of abPPO4, thus resulting in very interesting crystal packing.
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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>
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Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal.,Mauracher SG, Molitor C, Al-Oweini R, Kortz U, Rompel A Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2301-15. doi:, 10.1107/S1399004714013777. Epub 2014 Aug 29. PMID:25195745<ref>PMID:25195745</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4oua" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Agaricus bisporus]]
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[[Category: Agaricus bisporus var. bisporus H97]]
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[[Category: Tyrosinase]]
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[[Category: Large Structures]]
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[[Category: Al-Oweini, R.]]
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[[Category: Al-Oweini R]]
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[[Category: Kortz, U.]]
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[[Category: Kortz U]]
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[[Category: Mauracher, St G.]]
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[[Category: Molitor C]]
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[[Category: Molitor, C.]]
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[[Category: Rompel A]]
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[[Category: Rompel, A.]]
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[[Category: StMauracher G]]
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[[Category: Anderson-evans-type polyoxometalate]]
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[[Category: Hetero-protein co-crystallization]]
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[[Category: Oxidoreductase]]
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[[Category: Ppo4]]
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[[Category: Type-3 copper protein]]
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[[Category: Tyrosinase]]
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[[Category: Tyrosinase maturation]]
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[[Category: Zymogen]]
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Current revision

Coexistent single-crystal structure of latent and active mushroom tyrosinase (abPPO4) mediated by a hexatungstotellurate(VI)

PDB ID 4oua

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