Related Experiment Video
Updated: Feb 18, 2026

Laboratory Techniques Used to Maintain and Differentiate Biotypes of Vibrio cholerae Clinical and Environmental Isolates
Published on: May 30, 2017
A molecular model of the Vibrio cholerae cytolysin transmembrane pore
Sergio Pantano1, Cesare Montecucco
1Venetian Institute of Molecular Medicine (VIMM),Via Orus 2, 35129, Padova, Italy. sergio.pantano@unipd.it
Abstract:
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.
Related Concept Videos
ATP Synthase: Structure
Structure of Porins
Membrane Asymmetry Regulating Transporters
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Porin Insertion in the Outer Mitochondrial Membrane
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Single-pass Transmembrane Proteins
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...

