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Chunnel vision
Author(s) -
Andersen Christian,
Hughes Colin,
Koronakis Vassilis
Publication year - 2000
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kvd075
Subject(s) - periplasmic space , bacterial outer membrane , outer membrane efflux proteins , inner membrane , efflux , escherichia coli , escherichia coli proteins , transport protein , bacteria , microbiology and biotechnology , membrane , biology , chemistry , biophysics , biochemistry , genetics , gene
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 α‐helical trans‐periplasmic cylinder (tunnel) embedded in the outer membrane by a contiguous β‐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.