Bacterial Adaptor Membrane Fusion Proteins and the Structurally Dissimilar Outer Membrane Auxiliary Proteins Have Exchanged Central Domains in -Proteobacteria
Figure 3
Comparison of the predicted properties of the OMA of S. meliloti ((a) and (b)) with the MFP of N. mobilis ((c) and (d)) (see Figure 1). (a) Average hydropathy (solid line) and amphipathicity (dotted line) plots for the OMA (WHAT program; [23]). (b) Secondary structure predictions for the same OMA (SOPMA program, [24]). (c) Secondary structure predictions for the MFP of N. mobilis. (d) Average hydropathy and amphipathicity plots for the same MFP. The two sequences were aligned using the GAP program ([21]; Figure 1) which was used to prove homology. The single peaks of hydrophobicity correspond to the N-terminal transmembrane signal helices present in both proteins. In (b) and (c), long vertical lines indicate regions of predicted -helix, intermediate length vertical lines indicate regions of -sheet, and shorter vertical lines indicate regions of random coil or -turn.
