Allured V S, Collier R J, Carroll S F, McKay D B
Proc Natl Acad Sci U S A. 1986 Mar;83(5):1320-4. doi: 10.1073/pnas.83.5.1320.
Exotoxin A of Pseudomonas aeruginosa is a secreted bacterial toxin capable of translocating a catalytic domain into mammalian cells and inhibiting protein synthesis by the ADP-ribosylation of cellular elongation factor 2. The protein is a single polypeptide chain of 613 amino acids. The x-ray crystallographic structure of exotoxin A, determined to 3.0-A resolution, shows the following: an amino-terminal domain, composed primarily of antiparallel beta-structure and comprising approximately half of the molecule; a middle domain composed of alpha-helices; and a carboxyl-terminal domain comprising approximately one-third of the molecule. The carboxyl-terminal domain is the ADP-ribosyltransferase of the toxin. The other two domains are presumably involved in cell receptor binding and membrane translocation.
铜绿假单胞菌外毒素A是一种分泌型细菌毒素，能够将一个催化结构域转运到哺乳动物细胞中，并通过细胞延伸因子2的ADP核糖基化作用抑制蛋白质合成。该蛋白质是一条由613个氨基酸组成的单多肽链。外毒素A的X射线晶体结构分辨率为3.0埃，显示如下：一个氨基末端结构域，主要由反平行β结构组成，约占分子的一半；一个由α螺旋组成的中间结构域；以及一个羧基末端结构域，约占分子的三分之一。羧基末端结构域是毒素的ADP核糖基转移酶。另外两个结构域可能参与细胞受体结合和膜转运。
