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

Journal Article · · Acta crystallographica. Section F, Structural biology communications
;  [1]; ;  [2];  [1]
  1. Universität Wien, Althanstrasse 14, 1090 Wien (Austria)
  2. Jacobs University, PO Box 750 561, 28759 Bremen (Germany)

Polyphenol oxidase 4 (PPO4) from the natural source A. bisporus was crystallized in its latent precursor form (pro-tyrosinase; Ser2–Thr565) using the 6-tungstotellurate(VI) salt Na{sub 6}[TeW{sub 6}O{sub 24}]·22H{sub 2}O as a crystallization additive. 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 Na{sub 6}[TeW{sub 6}O{sub 24}]·22H{sub 2}O as a co-crystallization agent.

OSTI ID:
22375675
Journal Information:
Acta crystallographica. Section F, Structural biology communications, Vol. 70, Issue Pt 2; Other Information: PMCID: PMC3936457; PMID: 24637771; PUBLISHER-ID: wd5229; OAI: oai:pubmedcentral.nih.gov:3936457; Copyright (c) Mauracher et al. 2014; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); ISSN 2053-230X
Country of Publication:
United States
Language:
English