The cytotoxic activity of some of the most pathogenic strains of Vibrio cholerae is associated with a cytolysin protein (VCC), which forms oligomeric transmembrane pores and changes the permeability of intestinal cells. We present here a model structure of the transmembrane pore of VCC based on sequence comparison with other pore-forming toxins. VCC is suggested to form a transmembrane beta-barrel pore with a relatively large trans vestibule region. Calculations of the electrostatic profile within the pore lumen provide a rationale for the low conductance and selectivity of the VCC ion channel.