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J Bacteriol. 1992 October; 174(20): 6432-6437

research-article

An alpha-helical hydrophobic hairpin as a specific determinant in protein-protein interaction occurring in Escherichia coli colicin A and B immunity systems.

V Geli and C Lazdunski

Centre de Biochemie et Biologie Moléculaire, Centre National de la Recherche Scientifique, Marseille, France.

ABSTRACT

A collection of chimeric pore-forming domains between colicins A and B was constructed to investigate the specific determinants responsible for recognition by the corresponding immunity proteins. The fusion sites in the hybrid proteins were positioned according to the three-dimensional structure of the soluble form of the colicin A pore-forming domain. The hydrophobic hairpin of colicin pore-forming domains, buried in the core of the soluble structure, was the main determinant recognized by the integral immunity proteins. The immunity protein function may require helix-helix recognition within the lipid bilayer.

J Bacteriol. 1992 October; 174(20): 6432-6437




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