Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao

Abstract The pathogenic fungi Moniliophthora perniciosa causes Witches’ Broom Disease (WBD) of cacao. The structure of MpPR-1i, a protein expressed by M. perniciosa when it infects cacao, are presented. This is the first reported de novo structure determined by single-wavelength anomalous dispersion...

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Autores principales:	Renata M. Baroni, Zhipu Luo, Rabih Darwiche, Elissa M. Hudspeth, Roger Schneiter, Gonçalo A. G. Pereira, Jorge M. C. Mondego, Oluwatoyin A. Asojo
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Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/cc88fea7f60d451aae260def9d1d8a86
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spelling	oai:doaj.org-article:cc88fea7f60d451aae260def9d1d8a862021-12-02T16:08:21ZCrystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao10.1038/s41598-017-07887-12045-2322https://doaj.org/article/cc88fea7f60d451aae260def9d1d8a862017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07887-1https://doaj.org/toc/2045-2322Abstract The pathogenic fungi Moniliophthora perniciosa causes Witches’ Broom Disease (WBD) of cacao. The structure of MpPR-1i, a protein expressed by M. perniciosa when it infects cacao, are presented. This is the first reported de novo structure determined by single-wavelength anomalous dispersion phasing upon soaking with selenourea. Each monomer has flexible loop regions linking the core alpha-beta-alpha sandwich topology that comprise ~50% of the structure, making it difficult to generate an accurate homology model of the protein. MpPR-1i is monomeric in solution but is packed as a high ~70% solvent content, crystallographic heptamer. The greatest conformational flexibility between monomers is found in loops exposed to the solvent channel that connect the two longest strands. MpPR-1i lacks the conserved CAP tetrad and is incapable of binding divalent cations. MpPR-1i has the ability to bind lipids, which may have roles in its infection of cacao. These lipids likely bind in the palmitate binding cavity as observed in tablysin-15, since MpPR-1i binds palmitate with comparable affinity as tablysin-15. Further studies are required to clarify the possible roles and underlying mechanisms of neutral lipid binding, as well as their effects on the pathogenesis of M. perniciosa so as to develop new interventions for WBD.Renata M. BaroniZhipu LuoRabih DarwicheElissa M. HudspethRoger SchneiterGonçalo A. G. PereiraJorge M. C. MondegoOluwatoyin A. AsojoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Renata M. Baroni Zhipu Luo Rabih Darwiche Elissa M. Hudspeth Roger Schneiter Gonçalo A. G. Pereira Jorge M. C. Mondego Oluwatoyin A. Asojo Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao
description	Abstract The pathogenic fungi Moniliophthora perniciosa causes Witches’ Broom Disease (WBD) of cacao. The structure of MpPR-1i, a protein expressed by M. perniciosa when it infects cacao, are presented. This is the first reported de novo structure determined by single-wavelength anomalous dispersion phasing upon soaking with selenourea. Each monomer has flexible loop regions linking the core alpha-beta-alpha sandwich topology that comprise ~50% of the structure, making it difficult to generate an accurate homology model of the protein. MpPR-1i is monomeric in solution but is packed as a high ~70% solvent content, crystallographic heptamer. The greatest conformational flexibility between monomers is found in loops exposed to the solvent channel that connect the two longest strands. MpPR-1i lacks the conserved CAP tetrad and is incapable of binding divalent cations. MpPR-1i has the ability to bind lipids, which may have roles in its infection of cacao. These lipids likely bind in the palmitate binding cavity as observed in tablysin-15, since MpPR-1i binds palmitate with comparable affinity as tablysin-15. Further studies are required to clarify the possible roles and underlying mechanisms of neutral lipid binding, as well as their effects on the pathogenesis of M. perniciosa so as to develop new interventions for WBD.
format	article
author	Renata M. Baroni Zhipu Luo Rabih Darwiche Elissa M. Hudspeth Roger Schneiter Gonçalo A. G. Pereira Jorge M. C. Mondego Oluwatoyin A. Asojo
author_facet	Renata M. Baroni Zhipu Luo Rabih Darwiche Elissa M. Hudspeth Roger Schneiter Gonçalo A. G. Pereira Jorge M. C. Mondego Oluwatoyin A. Asojo
author_sort	Renata M. Baroni
title	Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao
title_short	Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao
title_full	Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao
title_fullStr	Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao
title_full_unstemmed	Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao
title_sort	crystal structure of mppr-1i, a scp/taps protein from moniliophthora perniciosa, the fungus that causes witches’ broom disease of cacao
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/cc88fea7f60d451aae260def9d1d8a86
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Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches’ Broom Disease of Cacao

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