title: Backbone and sidechain (1)H, (13)C and (15)N chemical shift assignments of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae.
abstract: Fungal hydrophobins are secreted proteins that self-assemble at hydrophobic:hydrophilic interfaces. They are essential for a variety of processes in the fungal life cycle, including mediating interactions with surfaces and infection of hosts. The fungus Magnaporthe oryzae, the causative agent of rice blast, relies on the unique properties of hydrophobins to infect cultivated rice as well as over 50 different grass species. The hydrophobin MPG1 is highly expressed during rice blast pathogenesis and has been implicated during host infection. Here we report the backbone and sidechain assignments for the class I hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae.
authors.affiliation: School of Molecular Bioscience, University of Sydney, Sydney, NSW, 2006, Australia.
authors.forename: Anthony A
authors.initials: AA
authors.lastname: Rey
authors.forename: Antoine
authors.initials: A
authors.lastname: Hocher
authors.forename: Ann H
authors.initials: AH
authors.lastname: Kwan
authors.forename: Margaret
authors.initials: M
authors.lastname: Sunde
mesh_terms: D000595:Amino Acid Sequence; D005656:Fungal Proteins / Q000737:chemistry*; D020082:Magnaporthe; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D012996:Solutions
chemical_list: D005656:Fungal Proteins; D012996:Solutions