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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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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Autor(es):
Baroni, Renata M. ; Luo, Zhipu ; Darwiche, Rabih ; Hudspeth, Elissa M. ; Schneiter, Roger ; Pereira, Goncalo A. G. ; Mondego, Jorge M. C. ; Asojo, Oluwatoyin A.
Número total de Autores: 8
Tipo de documento: Artigo Científico
Fonte: SCIENTIFIC REPORTS; v. 7, AUG 10 2017.
Citações Web of Science: 6
Resumo

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-betaalpha sandwich topology that comprise similar to 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 similar to 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. (AU)

Processo FAPESP: 10/52636-8 - Caracterizacao funcional e estrutural de proteinas similares a proteinas pr-1 expressas por moniliophthora perniciosa, fungo causador da vassoura de bruxa do cacaueiro.
Beneficiário:Renata Moro Baroni
Modalidade de apoio: Bolsas no Brasil - Doutorado
Processo FAPESP: 09/50119-9 - Estudo integrado e comparativo de três doenças fúngicas do cacau: vassoura-de-bruxa, monilíase e mal do facão, visando à compreensão de mecanismos de patogenicidade para o desenvolvimento de estratégias de controle
Beneficiário:Gonçalo Amarante Guimarães Pereira
Modalidade de apoio: Auxílio à Pesquisa - Temático