Crystal structure of colicin Ia

Abstract

The ion-channel forming colicins A, B, El, Ia, Ib and N all kill bacterial cells selectively by co-opting bacterial active-transport pathways and forming voltage-gated ion conducting channels across the plasma membrane of the target bacterium^1,2. The crystal structure of colicin Ia reveals a molecule 210 Å long with three distinct functional domains arranged along a backbone of two extraordinarily long α-helices. A central domain at the bend of the hairpin-like structure mediates specific recognition and binding to an outer-membrane receptor³. A second domain mediates translocation across the outer membrane via the TonB transport pathway⁴; the TonB-box⁵ recognition element of colicin Ia is on one side of three 80 Å-long helices arranged as a helical sheet. A third domain is made up of 10 α-helices which form a voltage-activated and voltage-gated ion conducting channel across the plasma membrane of the target cell. The two 160 Å-long α-helices that link the receptor-binding domain to the other domains enable the colicin Ia molecule to span the periplasmic space and contact both the outer and plasma membranes simultaneously during function^6,7.