Crystallization and preliminary X-ray crystallographic analysis of polyphenol oxidase from Juglans regia (jrPPO1)
- Universität Wien, Althanstrasse 14, 1090 Wien (Austria)
The crystallization and preliminary X-ray crystallographic analysis of a plant PPO exhibiting monophenolase activity from J. regia (jrPPO1) in its active form (Asp{sup 101}–Arg{sup 445}) are reported. Tyrosinase is a type 3 copper enzyme that catalyzes the ortho-hydroxylation of monophenols to diphenols as well as their subsequent oxidation to quinones, which are precursors for the biosynthesis of melanins. The first plant tyrosinase from walnut leaves (Juglans regia) was purified to homogeneity and crystallized. During the purification, two forms of the enzyme differing only in their C-termini [jrPPO1(Asp{sup 101}–Pro{sup 444}) and jrPPO1(Asp{sup 101}–Arg{sup 445})] were obtained. The most abundant form jrPPO1(Asp{sup 101}–Arg{sup 445}), as described in Zekiri et al. [Phytochemistry (2014 ▶), 101, 5–15], was crystallized, resulting in crystals that belonged to space group C121, with unit-cell parameters a = 115.56, b = 91.90, c = 86.87 Å, α = 90, β = 130.186, γ = 90°, and diffracted to 2.39 Å resolution. Crystals were only obtained from solutions containing at least 30% polyethylene glycol 5000 monomethyl ether in a close-to-neutral pH range.
- OSTI ID:
- 22375690
- Journal Information:
- Acta crystallographica. Section F, Structural biology communications, Vol. 70, Issue Pt 6; Other Information: PMCID: PMC4051548; PMID: 24915104; PUBLISHER-ID: ub5057; OAI: oai:pubmedcentral.nih.gov:4051548; Copyright (c) Zekiri 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
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