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Article

A periplasmic coiled-coil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumps.

Proceedings of the National Academy of Sciences of the United States of America - 13 Mar 2007

Lobedanz Sune, Bokma Evert, Symmons Martyn F, Koronakis Eva, Hughes Colin, Koronakis Vassilis

Abstract excerpt

Bacteria such as Escherichia coli and Pseudomonas aeruginosa expel antibiotics and other inhibitors via tripartite multidrug efflux pumps spanning the inner and outer membranes and the intervening periplasmic space. A key event in pump assembly is the recruitment of an outer membrane-anchored TolC exit duct by the adaptor protein of a cognate inner membrane translocase, establishing a contiguous transenvelope...

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Identifiers

PMID: 17360572
DOI: 10.1073/pnas.0610160104
PMCID: PMC1838649

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A periplasmic coiled-coil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumps.PMID 17360572Read ↗

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Elucidating TolC Protein Dynamics: Structural Shifts Facilitate Efflux Mediated β-lactam ResistanceSemantic proximity Read ↗

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Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli.Semantic proximity Read ↗

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