Figure 4
Conserved dynamics of the aerolysin-like proteins. (a) RMS fluctuations per residue in the PF region (corresponding to residues 195–310 of aerolysin), during the MD trajectory of each toxin: aerolysin wt (red), aerolysin Y221G (black), ETX wt (green), ETX H162A (blue), parasporin-2 (magenta) and LSL (cyan). (b–d) Three main monomer motions (PCs) as obtained from the PCA, superposed with the monomer (green), prepore (magenta) and pore (red) aerolysin structures. The three main motions are represented by the two extreme projections along the MD trajectory on the average structure of aerolysin Y221G (shown in yellow and cyan): PC1 (b); PC2 (c), in a look-up of domain 4, showing that one of the extreme projections superposes with domain 4 in the pore state, while the other resembles the soluble state; and PC3 (d), in a look-up of domain 3, showing the motion of strands β3 and β5 that lead to their parallel disposition in the prepore oligomer. (e) Correlated (left) and anti-correlated (right) residues depicted with red and blue lines, respectively, as calculated from the aerolysin wt MD trajectory. (f) Decreased cross-correlations between the wt and the mutant forms for aerolysin (left) and ETX (right). The aromatic amino acid that holds the mutation is shown.
