Fig 1. Conservation in TM3B in Ec-MscS.

A) Structural representation of the five residues (S114, red; L118, blue; A120, lime green; L123, aqua; F127, magenta) on the open state crystal structure, black lines indicate the predicted location of the lipid headgroups. B) A close-up of the location of these residues is shown, for clarity only two adjacent subunits are shown. C) A conservation map of TM3B comparing the amino acid sequence of Ec-MscS with the residues of highest conservation within the MscS superfamily. Larger amino acids indicate higher conservation at that residue, the y-axis in bits gives the maximum sequence conservation, log₂(20) = 4.13. Hydrophobic residues (I, P, L, M, V, A, G), are colored black; aromatic residues (F, W, Y) are colored red; polar residues (S, T, Q, N, C) are colored blue; basic residues (K, R, H) are colored green; and acidic residues (D, E) are colored yellow. E. coli MscS residues that are significantly different from the conserved residue are indicated with a ■ below, in colors corresponding to the structural representation.