| Literature DB >> 11269495 |
C Andersen1, C Hughes, V Koronakis.
Abstract
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.Entities:
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Year: 2000 PMID: 11269495 PMCID: PMC1083749 DOI: 10.1093/embo-reports/kvd075
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807