Fig. 3.

Evolutionary conservation of the dimerization interfaces of She4p. (A) The three dimerization interfaces are indicated with blue and red dotted lines, with molecule A in green and molecule B in purple; N and C indicate N and C termini, respectively. Boxed portions indicate apposing dimerization surfaces of the two short arms of L. (B–G) Dimerization surfaces of the two short arms of the L-shaped A and B molecules are colored according to electrostatic potential (with saturating blue and red at ± 15 kT/e). (B and E) Conservation between related fungal homologues (yellow) (C and F); or, hydrophobicity (green) (D and G); black lines encircle conserved regions. (H–J) Symmetry-related dimerization interfaces between the N-helices and the contra-lateral bend of the L-shaped A and B molecules (see Fig. 2A); the N helix of molecule A was superimposed as a ribbon with stick and ball side chains onto the surface of the bend of molecule B; conserved residues of the helix are indicated in cyan; otherwise the coloring of the electrostatic, conserved, and hydrophobic surfaces of the bend of L is as in B–G. (K) Electron density of the N helix. The composite omit map (2fo-fc) covering the N helix of molecule A is shown in blue mesh. The map was contoured at 1σ cutoff. The refined N helix is shown in stick and ball model with residue names and numbers labeled. The bend of molecule B is shown in surface representation.