Yin Y, Zhang F, Ling V, Arrowsmith C H
Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.
FEBS Lett. 1995 Jun 5;366(1):1-5. doi: 10.1016/0014-5793(95)00454-h.
NMR spectroscopy was used to study the structure of the C-terminal signal sequences of the bacterial toxins, hemolysin A(HlyA) and leukotoxin A (LktA). The two signals share little sequence homology; however, both can direct toxin transport with equal efficiency. We report here that in a membrane mimetic environment both peptides form two short non-interacting alpha-helices separated by a short loop. This higher order structure may be a common feature of C-terminal signals and may be required for interaction with the membrane associated transporter complex.
核磁共振光谱法被用于研究细菌毒素溶血素A（HlyA）和白细胞毒素A（LktA）的C端信号序列的结构。这两个信号的序列同源性很低；然而，两者都能以相同的效率引导毒素转运。我们在此报告，在模拟膜环境中，这两种肽都形成了由一个短环隔开的两个短的、不相互作用的α螺旋。这种高阶结构可能是C端信号的一个共同特征，可能是与膜相关转运复合物相互作用所必需的。
