TolC – the bacterial exit duct for proteins and drugs

FEBS Letters

Koronakis, Vassilis¹ 

[1] Cambridge University Department of Pathology, Tennis Court Road, Cambridge CB2 1QP, UK

关键词: Protein export;    Membrane protein;    Multidrug resistance;    Drug efflux;   

DOI  :  10.1016/S0014-5793(03)01125-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The TolC structure has unveiled a common mechanism for the movement of molecules, large and small, from the bacterial cell cytosol, across two membranes and the intervening periplasm, into the environment. Trimeric TolC is a remarkable cell exit duct that differs radically from other membrane proteins, comprising a 100-Å long α-barrel that projects across the periplasmic space, anchored by a 40-Å long β-barrel spanning the outer membrane. The periplasmic entrance of TolC is closed until recruitment by substrate-specific translocases in the inner membrane triggers its transition to the open state, achieved by an iris-like ‘untwisting’ of the tunnel α-helices. TolC-dependent machineries present ubiquitous exit routes for virulence proteins and antibacterial drugs, and their conserved structure, specifically the electronegative TolC entrance constriction, may present a target for inhibitors of multidrug-resistant pathogens.

【 授权许可】

Unknown