Figure 3
Physicochemical and coevolution constraints to variability within the aerolysin-like family. (a,b) Conserved amino acid physiochemical properties, mapped on the double β-barrel region of the pore structure in (a) or in the soluble monomer in (b): magenta = preference for small volumes (suggests flexibility is required), green = preference for hydrophilic amino acids, blue = preference for soluble amino acids, black = preference for hydrophobic amino acids, yellow = preference for metabolically inexpensive amino acids, orange = distributions shape by backbone conformational descriptors (labeled and shown as spheres in b). In cyan, residues highly conserved from Fig. 2. Magenta boxes show the residues of the hinge between the stem loop and strands β2-β3. (c–e) Coevolution-predicted contacts above the noise level for the aerolysin-like family, calculated from the sequence alignment retrieved using as target the aerolysin sequence from 190–315, and compared to contact maps for aerolysin in the monomer (c) prepore (d) and pore structures (e). Black dots mark pairs of coevolving residues, the contact map in light blue corresponds to intra-monomer contacts from the structures, and the contact map in magenta corresponds to inter-monomer contacts. The double β-barrel (DBB) and stem loop (SL) regions are represented on the sequence. The coevolution patterns mentioned within the text are highlighted with colored ellipses.
