Figure 6
Limited electrostatic contributions of colicin/pyocin residues to interactions with the α2 helix and adjacent residues in immunity proteins. Colicin residues that substantially contribute electrostatically to interactions with the Im α2 helix are shown as sticks and colored according to their energy contributions, as in Fig. 5. Colicin residues that contribute similarly to interactions across multiple members are marked with diamonds and colored as follows (the corresponding E7 position number, as in Fig. 3B, is also noted): purple (E7#531), red (E7#534), light blue (E7#539), and green (E7#528 or E7#540). Colicin residues that contribute to interactions with the cognate immunity protein only in one complex are marked with black triangles. The colicin/pyocin α2 helices are colored orange, the α4 helices are colored teal, and the α4–β2 loops are colored green. Colicin/pyocin structures are rotated 35° about the Y-axis relative to Fig. 5.
