Molecular dynamics simulation of mutant
fragaceatoxin C nanopores.
(A–C) All-atom models of WtFraC-T1 (A), G13F-FraC-T1 (B), and
WtFraC-T2 (C) nanopores. The protein is shown as a gray cutaway surface,
embedded in a DPhPC lipid bilayer (blue). The G13F mutation site in
panel b is shown in red. All systems contain 1 M KCl solution (potassium
in orange and chloride in green, water not shown). The protonation
states of the titratable residues are set to reflect the pH of 3.8.
The z axis is shown on the left for scale. Yellow
and red horizontal lines show the position of the electrostatic minima
and maxima, respectively. (D) Experimental and simulated open pore
currents at −50 mV for the three systems. The simulated values
reflect scaling of the raw MD current with the ratio of the experimental
and simulated bulk conductivity of 1 M KCl. The error bars represent
the standard error computed by splitting the MD trajectories into
10 ns fragments and considering each fragment as an independent measurement
of the current. The contribution of the potassium ion to the MD current
is specified at the bottom. (E) Average electrostatic potential along
the symmetry axis (z axis) of the three pores. (F,
G) Profiles of potassium (F) and chloride (G) ion concentration along
the symmetry axis of each nanopore.