An alpha-helical hydrophobic hairpin as a specific determinant in protein-protein interaction occurring in Escherichia coli colicin A and B immunity systems.
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.
Geli
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V
Centre de Biochemie et Biologie Moléculaire, Centre National de la Recherche Scientifique, Marseille, France.
Lazdunski
C
C
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D003001:Cloning, Molecular; D003087:Colicins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010957:Plasmids / Q000235:genetics; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D011995:Recombination, Genetic / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; D003087:Colicins; D046911:Macromolecular Substances; D011993:Recombinant Fusion Proteins; C007104:colicin immunity proteins