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Article

Gating movements of colicin A and colicin Ia are different.

The Journal of membrane biology - 1 Nov 2004

Slatin S L, Duché D, Kienker P K, Baty D

Abstract excerpt

Both colicin A and colicin Ia belong to a subfamily of the bacterial colicins that act by forming a voltage-dependent channel in the inner membrane of target bacteria. Both colicin A and Ia open at positive and close at negative potential, but only colicin A exhibits distinctly biphasic turnoff kinetics, implying the existence of two open states. Previous work has shown that Colicin Ia gating is associated with...

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Identifiers

PMID: 15702371
DOI: 10.1007/s00232-004-0720-9

Provenance

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.

Related research

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Research trail→

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Gating movements of colicin A and colicin Ia are different.PMID 15702371Read ↗

Protein translocation across planar bilayers by the colicin Ia channel-forming domain: where will it end?Semantic proximity Read ↗

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Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli.Semantic proximity Read ↗

Membrane topology of the colicin E1 channel using genetically encoded fluorescence.Semantic proximity Read ↗

Energetics of colicin import revealed by genetic cross-complementation between the Tol and Ton systems.Semantic proximity Read ↗

Quantification of group A colicin import sites.Semantic proximity Read ↗

Identification of a translocated gating charge in a voltage-dependent channel. Colicin E1 channels in planar phospholipid bilayer membranes.Semantic proximity Read ↗

Protein import into Escherichia coli: colicins A and E1 interact with a component of their translocation system.Semantic proximity Read ↗

Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli.Semantic proximity Read ↗

Adventures in membrane protein topology. A study of the membrane-bound state of colicin E1.Semantic proximity Read ↗

Domains of colicin M involved in uptake and activity.Semantic proximity Read ↗

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