Purification and characterization of tobacco pathogenesis-related protein PR-5d, an antifungal thaumatin-like protein.
Cultured tobacco cells accumulate several pathogenesis-related proteins. A neutral PR-5 protein, PR-5d, was purified to homogeneity from such cells. PR-5d has highly hydrophobic characteristics, but hydropathy analysis of its primary structure did not show a hydrophobic domain. In a series of bioassays, purified PR-5d showed inhibitory activity against several phytopathogenic and non-phytopathogenic fungi as do other members of the PR-5 protein family. To study the antifungal mechanism based on three dimensional structure of PR-5d, purified PR-5d was crystallized. The preliminary X-ray analysis of the crystal revealed that the crystals belong to space group C2, with cell dimensions a = 80.2 A, b = 63.8 A, c = 45.7 A, and beta = 107.2 degrees, and diffract at least 1.8 A resolution.
Koiwa
H
H
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
Kato
H
H
Nakatsu
T
T
Oda
J
J
Yamada
Y
Y
Sato
F
F
D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000737:chemistry* / Q000494:pharmacology; D001681:Biological Assay; D002478:Cells, Cultured; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000494:pharmacology; D010947:Plants, Toxic; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013549:Sweetening Agents; D014026:Nicotiana / Q000737:chemistry* / Q000166:cytology
D000935:Antifungal Agents; D010940:Plant Proteins; D013549:Sweetening Agents; C053376:pathogenesis-related proteins, plant; C003427:thaumatin protein, plant