烟草病程相关蛋白PR-5d（一种抗真菌类甜蛋白）的纯化与特性分析
Purification and characterization of tobacco pathogenesis-related protein PR-5d, an antifungal thaumatin-like protein.
作者信息
Koiwa H, Kato H, Nakatsu T, Oda J, Yamada Y, Sato F
机构信息
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
出版信息
Plant Cell Physiol. 1997 Jul;38(7):783-91. doi: 10.1093/oxfordjournals.pcp.a029236.
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.
培养的烟草细胞会积累多种病程相关蛋白。一种中性病程相关蛋白5（PR - 5），即PR - 5d，从这些细胞中被纯化至同质。PR - 5d具有高度疏水的特性，但其一级结构的亲水性分析并未显示出疏水结构域。在一系列生物测定中，纯化的PR - 5d与PR - 5蛋白家族的其他成员一样，对几种植物病原真菌和非植物病原真菌表现出抑制活性。为了基于PR - 5d的三维结构研究其抗真菌机制，纯化的PR - 5d被结晶。对该晶体的初步X射线分析表明，晶体属于空间群C2，晶胞参数为a = 80.2 Å，b = 63.8 Å，c = 45.7 Å，β = 107.2°，并且至少在1.8 Å分辨率下产生衍射。
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