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Crystallization and preliminary X-ray crystallographic analysis of latent isoform PPO4 mushroom (Agaricus bisporus) tyrosinase

DOI: 10.1107/S2053230X14000582 DOI Help
PMID: 24637771 PMID Help

Authors: Stephan Mauracher (University of Vienna) , Annette Rompel (Universitat Wien) , Rami Al-oweini (Jacobs University) , Ulrich Kortz (Jacobs University) , Christian Molitor (Institut für Biophysikalische Chemie, Fakultät für Chemie, Universität Wien)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 (2) , PAGES 263-266

State: Published (Approved)
Published: February 2014
Diamond Proposal Number(s): 8476

Open Access Open Access

Abstract: 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 Å resolution. The protein only formed crystals under low-salt conditions using the 6-tungstotellurate(VI) salt Na6[TeW6O24]·22H2O as a co-crystallization agent.

Journal Keywords: tyrosinases; zymogens; polyphenol oxidase 4; Agaricus bisporus; polyoxometalates

Subject Areas: Chemistry

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 20/01/2014 17:32

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