Abstract
Colicin Ia is a bactericidal protein that kills E. coli by making a voltage-dependent ion channel in their inner membrane and de-energizing them. To do this, the colicin or its pore-forming domain must cross the outer bacterial membrane. Like all colicins, Ia first binds to an outer membrane receptor. The crystal structure of colicin Ia bound to its outer membrane receptor, the 22-strand plugged β-barrel protein, Cir, suggests the plug doesn't move upon Ia binding. Therefore, another pathway is needed for the colicin to cross the outer membrane.
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