Figure 2
Sequence conservation within the aerolysin-like family. (a) Number of sequences counts for the full aerolysin sequence or only the segment 190–315, where a count is defined as a position with no gap on the alignment. Above the alignment, the aerolysin conserved structural regions are reported in bars colored according to Fig. 1. (b) Weblogo diagram of amino acid conservation computed from the alignment of the segment 190–315. (c) Amino acid variability from 1 (blue, strictly conserved) to 20 (red, highly variable), mapped on the aerolysin double β-barrel region. In the left, the exterior pore surface is shown and, in the right, the surface has been cut to show the pore lumen. (d) Aerolysin pore structure, with only one protomer colored according to: MB domain in black, segment 190–309 in yellow, segment 310–315 in blue, segment 408–421 (β5 strand) in green. The most conserved amino acids are shown as red sticks. The MB domains in the front have been removed to improve visualization. (e) Aerolysin soluble monomer structure, with the same coloring scheme as in (d).
