On the role of lipid in colicin pore formation.
On the role of lipid in colicin pore formation.
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关于脂质在大肠杆菌素孔形成中的作用。
DOI：
10.1016/j.bbamem.2004.07.001
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
Cramer,WilliamA
中科院分区：
文献类型：
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作者：
Zakharov,StanislavD;Kotova,ElenaA;Antonenko,YuriN;Cramer,WilliamA
关于蛋白质-膜相互作用的见解，其中大肠杆菌素的C-末端成孔结构域插入膜并形成电压门控通道，以及大肠杆菌素通道的性质，通过以下数据提供：（i）流体阴离子膜界面层中大肠杆菌素成孔域的柔性螺旋伸长状态，用于通道形成的最佳阴离子表面电荷，和电压门控易位的大肠杆菌素结构域的带电区域跨膜;（ii）结构-功能数据的电压门控K+通道显示易位的富含精氨酸的螺旋片段通过膜;（iii）环形通道形成的小肽，涉及本地参与的阴离子脂质在一个反相。有人提出，跨膜的大肠杆菌素的易位发生通过最小化的玻恩充电能量的带正电荷的碱性残基跨脂质双层的中和与阴离子脂质头基团的易位。所得的孔结构可以由稍微短的，约。16个残基，跨膜螺旋，在局部变薄的膜，连同反相脂质胶束的表面元素。
Insights into the protein–membrane interactions by which the C-terminal pore-forming domain of colicins inserts into membranes and forms voltage-gated channels, and the nature of the colicin channel, are provided by data on: (i) the flexible helix-elongated state of the colicin pore-forming domain in the fluid anionic membrane interfacial layer, the optimum anionic surface charge for channel formation, and voltage-gated translocation of charged regions of the colicin domain across the membrane; (ii) structure–function data on the voltage-gated K+channel showing translocation of an arginine-rich helical segment through the membrane; (iii) toroidal channels formed by small peptides that involve local participation of anionic lipids in an inverted phase. It is proposed that translocation of the colicin across the membrane occurs through minimization of the Born charging energy for translocation of positively charged basic residues across the lipid bilayer by neutralization with anionic lipid head groups. The resulting pore structure may consist of somewhat short, ca. 16 residues, trans-membrane helices, in a locally thinned membrane, together with surface elements of inverted phase lipid micelles.