Purification and characterization of tobacco pathogenesis-related protein PR-5d, an antifungal thaumatin-like protein. Academic Article

abstract

• 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.

authors

• Koiwa, Hisashi

published proceedings

• Plant Cell Physiol

altmetric score

• 6

author list (cited authors)

• Koiwa, H., Kato, H., Nakatsu, T., Oda, J., Yamada, Y., & Sato, F.

citation count

• 53

complete list of authors

• Koiwa, H||Kato, H||Nakatsu, T||Oda, J||Yamada, Y||Sato, F

publication date

• July 1997

publisher

• Oxford University Press (OUP)  Publisher

published in

• Plant and Cell Physiology  Journal

keywords

• Amino Acid Sequence
• Antifungal Agents
• Biological Assay
• Cells, Cultured
• Circular Dichroism
• Crystallography, X-Ray
• Molecular Sequence Data
• Plant Proteins
• Plants, Toxic
• Sequence Analysis
• Sequence Homology, Amino Acid
• Sweetening Agents
• Tobacco

PubMed Central ID

• 9297844

Digital Object Identifier (DOI)

• 10.1093/oxfordjournals.pcp.a029236

start page

• 783

end page

• 791

volume

• 38

issue

• 7

URL

• http%3A%2F%2Fdx.doi.org%2F10.1093%2Foxfordjournals.pcp.a029236

user-defined tag

• 3 Good Health and Well-Being