Crystal structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa , the fungus that causes witches’ broom disease of cacao

Baroni, Renata Moro; Luo, Zhipu; Darwiche, Rabih; Hudspeth, Elissa M.; Schneiter, Roger; Pereira, Gonçalo A. G.; Mondego, Jorge M. C.; Asojo, Oluwatoyin A.

doi:10.1038/s41598-017-07887-1

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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

Baroni, Renata Moro Genomics and Expression Laboratory (LGE), Institute of Biology, UNICAMP, Campinas, Brazil - Agronomic Institute (IAC), Campinas, Brazil
Luo, Zhipu Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne, USA
Darwiche, Rabih Department of Biology, University of Fribourg, Switzerland
Hudspeth, Elissa M. National School of Tropical Medicine, Baylor College of Medicine, Houston, USA
Schneiter, Roger Department of Biology, University of Fribourg, Switzerland
Pereira, Gonçalo A. G. Genomics and Expression Laboratory (LGE), Institute of Biology, UNICAMP, Campinas, Brazil
Mondego, Jorge M. C. Agronomic Institute (IAC), Campinas, Brazil
Asojo, Oluwatoyin A. National School of Tropical Medicine, Baylor College of Medicine, Houston, USA

10.08.2017

Published in:

Scientific Reports. - 2017, vol. 7, no. 1, p. 7818

English 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.

Faculty

Faculté des sciences et de médecine

Department

Département de Biologie

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