Andersen C, Hughes C, Koronakis V
University of Cambridge Department of Pathology, UK.
EMBO Rep. 2000 Oct;1(4):313-8. doi: 10.1093/embo-reports/kvd075.
The Escherichia coli TolC protein is central to toxin export and drug efflux across the inner and outer cell membranes and the intervening periplasmic space. The crystal structure has revealed that TolC assembles into a remarkable alpha-helical trans-periplasmic cylinder (tunnel) embedded in the outer membrane by a contiguous beta-barrel (channel), so providing a large duct open to the outside environment. The channel-tunnel structure is conserved in TolC homologues throughout Gram-negative bacteria, and it is envisaged that they are recruited and opened, through a common mechanism, by substrate-specific inner-membrane complexes.
大肠杆菌TolC蛋白对于毒素穿过内膜和外膜以及其间的周质空间进行输出以及药物外排至关重要。晶体结构显示,TolC组装成一个显著的α螺旋跨周质圆柱体(通道),该圆柱体通过连续的β桶(通道)嵌入外膜,从而形成一个通向外部环境的大管道。通道-圆柱体结构在整个革兰氏阴性菌的TolC同源物中是保守的,据设想,它们通过一种共同机制被底物特异性内膜复合物募集并打开。