A molecular model of the Vibrio cholerae cytolysin transmembrane pore.
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.
Pantano
Sergio
S
Venetian Institute of Molecular Medicine (VIMM),Via Orus 2, 35129, Padova, Italy. sergio.pantano@unipd.it
Montecucco
Cesare
C
D000465:Algorithms; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism*; D002463:Cell Membrane Permeability; D004553:Electric Conductivity; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008956:Models, Chemical; D008969:Molecular Sequence Data; D054353:Perforin; D052899:Pore Forming Cytotoxic Proteins; D016062:Porosity; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity; D014734:Vibrio cholerae / Q000737:chemistry*
D001426:Bacterial Proteins; D007473:Ion Channels; D008562:Membrane Glycoproteins; D052899:Pore Forming Cytotoxic Proteins; D054353:Perforin