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Article

Solution Structure, Dynamics, and New Antifungal Aspects of the Cysteine-Rich Miniprotein PAFC

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Department of Organic Chemistry, Faculty of Science and Technology, University of Debrecen, H-4032 Debrecen, Hungary
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Institute of Molecular Biology, Biocenter, Medical University of Innsbruck, A-6020 Innsbruck, Austria
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Institute of Plant Biology, Biological Research Centre, Eötvös Loránd Research Network, H-6726 Szeged, Hungary
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Department of Biotechnology, Faculty of Science and Informatics, University of Szeged, H-6726 Szeged, Hungary
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Department of Plant Biology, Faculty of Sciences and Informatics, University of Szeged, H-6726 Szeged, Hungary
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Department of Medical Chemistry, Faculty of Medicine, University of Szeged, H-6720 Szeged, Hungary
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Institute of Biochemistry, Biological Research Centre, Eötvös Loránd Research Network, H-6726 Szeged, Hungary
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MTA-SZTE Biomimetic Systems Research Group, University of Szeged, Dóm tér 8, H-6720 Szeged, Hungary
*
Authors to whom correspondence should be addressed.
These authors share first authorship.
Int. J. Mol. Sci. 2021, 22(3), 1183; https://doi.org/10.3390/ijms22031183
Received: 30 December 2020 / Revised: 18 January 2021 / Accepted: 20 January 2021 / Published: 25 January 2021
(This article belongs to the Section Macromolecules)
The genome of Penicillium chrysogenum Q176 contains a gene coding for the 88-amino-acid (aa)-long glycine- and cysteine-rich P. chrysogenum antifungal protein C (PAFC). After maturation, the secreted antifungal miniprotein (MP) comprises 64 aa and shares 80% aa identity with the bubble protein (BP) from Penicillium brevicompactum, which has a published X-ray structure. Our team expressed isotope (15N, 13C)-labeled, recombinant PAFC in high yields, which allowed us to determine the solution structure and molecular dynamics by nuclear magnetic resonance (NMR) experiments. The primary structure of PAFC is dominated by 14 glycines, and therefore, whether the four disulfide bonds can stabilize the fold is challenging. Indeed, unlike the few published solution structures of other antifungal MPs from filamentous ascomycetes, the NMR data indicate that PAFC has shorter secondary structure elements and lacks the typical β-barrel structure, though it has a positively charged cavity and a hydrophobic core around the disulfide bonds. Some parts within the two putative γ-core motifs exhibited enhanced dynamics according to a new disorder index presentation of 15N-NMR relaxation data. Furthermore, we also provided a more detailed insight into the antifungal spectrum of PAFC, with specific emphasis on fungal plant pathogens. Our results suggest that PAFC could be an effective candidate for the development of new antifungal strategies in agriculture. View Full-Text
Keywords: Penicillium chrysogenum; antifungal protein PAFC; γ-core motif; solution structure; dynamics; nuclear magnetic resonance; plant protection Penicillium chrysogenum; antifungal protein PAFC; γ-core motif; solution structure; dynamics; nuclear magnetic resonance; plant protection
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MDPI and ACS Style

Czajlik, A.; Holzknecht, J.; Galgóczy, L.; Tóth, L.; Poór, P.; Ördög, A.; Váradi, G.; Kühbacher, A.; Borics, A.; Tóth, G.K.; Marx, F.; Batta, G. Solution Structure, Dynamics, and New Antifungal Aspects of the Cysteine-Rich Miniprotein PAFC. Int. J. Mol. Sci. 2021, 22, 1183. https://doi.org/10.3390/ijms22031183

AMA Style

Czajlik A, Holzknecht J, Galgóczy L, Tóth L, Poór P, Ördög A, Váradi G, Kühbacher A, Borics A, Tóth GK, Marx F, Batta G. Solution Structure, Dynamics, and New Antifungal Aspects of the Cysteine-Rich Miniprotein PAFC. International Journal of Molecular Sciences. 2021; 22(3):1183. https://doi.org/10.3390/ijms22031183

Chicago/Turabian Style

Czajlik, András, Jeanett Holzknecht, László Galgóczy, Liliána Tóth, Péter Poór, Attila Ördög, Györgyi Váradi, Alexander Kühbacher, Attila Borics, Gábor K. Tóth, Florentine Marx, and Gyula Batta. 2021. "Solution Structure, Dynamics, and New Antifungal Aspects of the Cysteine-Rich Miniprotein PAFC" International Journal of Molecular Sciences 22, no. 3: 1183. https://doi.org/10.3390/ijms22031183

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