Klebba P E, Rutz J M, Liu J, Murphy C K
Department of Microbiology, Medical College of Wisconsin, Milwaukee 53226.
J Bioenerg Biomembr. 1993 Dec;25(6):603-11. doi: 10.1007/BF00770247.
The recent solution of enteric bacterial porin structure, and new insights into the mechanism by which outer membrane receptor proteins recognize and internalize specific ligands, advocates the re-evaluation of TonB-dependent transport physiology. In this minireview we discuss the potential structural features of siderophore receptors and TonB, and use this analysis to evaluate both existing and new models of energy and signal transduction from the inner membrane to the outer membrane of gram-negative bacteria.
近期肠道细菌孔蛋白结构的解析，以及对外膜受体蛋白识别并内化特定配体机制的新认识，促使人们重新评估依赖TonB的转运生理学。在这篇微型综述中，我们讨论了铁载体受体和TonB的潜在结构特征，并利用这一分析来评估革兰氏阴性菌从内膜到外膜的能量和信号转导的现有模型和新模型。
