Ectatomin (Ea) is a newly isolated main toxic component of Ectatomma t
uberculatum ant venom. Structural and electrophysiological studies wer
e performed with purified Ea. The protein consists of two homologous p
olypeptide chains (37 and 34 residues) and forms a four alpha-helix bu
ndle in aqueous solution. On insertion into artificial bilayer membran
es, two Ea molecules form an ion pore. Our results suggest that the 'i
nside-out' mechanism of pore formation requires a significant movement
of Ea helical parts. The pore formation in the cell membrane might we
ll explain the toxic activity of Ea, not excluding at the same time it
s intracellular activities.