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- W1996452607 abstract "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-A long alpha-barrel that projects across the periplasmic space, anchored by a 40-A long beta-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 alpha-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." @default.
- W1996452607 created "2016-06-24" @default.
- W1996452607 creator A5026123454 @default.
- W1996452607 date "2003-10-08" @default.
- W1996452607 modified "2023-10-17" @default.
- W1996452607 title "TolC - the bacterial exit duct for proteins and drugs" @default.
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- W1996452607 doi "https://doi.org/10.1016/s0014-5793(03)01125-6" @default.
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