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

doi:10.1128/JB.180.16.4111-4115.1998

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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...

Topics

Amino Acid Sequence
Bacterial Proteins
Binding Sites
Cell Membrane
Colicins
Molecular Sequence Data
Mutation
Protein Conformation
Sequence Alignment
Sequence Homology, Amino Acid
Shigella boydii

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