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Article

The tip of the hydrophobic hairpin of colicin U is dispensable for colicin U activity but is important for interaction with the immunity protein.

Journal of bacteriology - 1 Aug 1998

Pilsl H, Smajs D, Braun V

Abstract excerpt

The hydrophobic C terminus of pore-forming colicins associates with and inserts into the cytoplasmic membrane and is the target of the respective immunity protein. The hydrophobic region of colicin U of Shigella boydii was mutated to identify determinants responsible for recognition of colicin U by the colicin U immunity protein. Deletion of the tip of the hydrophobic hairpin of colicin U resulted in a fully...

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Identifiers

PMID: 9696757
DOI: 10.1128/JB.180.16.4111-4115.1998
PMCID: PMC107405

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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.

Related research

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The tip of the hydrophobic hairpin of colicin U is dispensable for colicin U activity but is important for interaction with the immunity protein.PMID 9696757Read ↗

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The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Semantic proximity Read ↗

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