STRUCTURE OF EXOTOXIN-A OF PSEUDOMONAS-AERUGINOSA AT 3.0-ANGSTROM RESOLUTION
STRUCTURE OF EXOTOXIN-A OF PSEUDOMONAS-AERUGINOSA AT 3.0-ANGSTROM RESOLUTION
复制标题
DOI：
10.1073/pnas.83.5.1320
复制
发表时间：
1986-03-01
影响因子：
11.1
通讯作者：
MCKAY, DB
中科院分区：
文献类型：
--
作者：
ALLURED, VS;COLLIER, RJ;MCKAY, DB
铜绿假单胞菌外毒素A是一种分泌型细菌毒素，能够将催化结构域转移到哺乳动物细胞中，并通过细胞延伸因子2的ADP-核糖基化抑制蛋白质合成。该蛋白质是613个氨基酸的单一多肽链。外毒素A的X-射线晶体结构，测定为3.0-.分辨率，显示如下：氨基末端结构域，主要由反平行的β-结构并包含大约一半的分子;由α-螺旋;和羧基末端结构域，其占分子的约三分之一。羧基末端结构域是毒素的ADP-核糖基转移酶。其他两个域可能参与细胞受体结合和膜转位。
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-.ANG. 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.