FIGURE 2.

Construction of the FliM_C homology model. An alignment of FliN and FliM C-terminal domains is shown in the upper panel. Boxes indicate positions where hydrophobic character is conserved, and asterisks indicate the positions forming the core in both FliN and the homology-modeled FliM_C. The solid line under the E. coli C-terminal sequence represents the residues that are included in the FliM_C homology model. FliN forms intertwined dimers, with topology sketched in the middle panel. Altered connectivity in two places (indicated in red) allows the FliM peptide to fold as a monomer (consistent with the known properties of FliM, which interacts with FliN to form 1:4 complexes). The homology model has conserved hydrophobic residues at core positions (shown in yellow in the lower panel). Ec-Nc and Ec-Mc, E. coli FliN and FliM C-terminal domains, respectively; Tma-Nc and Tma-Mc, T. maritima FliN and FliM C-terminal domains, respectively; Bbu-Nc and Bbu-Mc, B. burgdorferi FliN and FliM C-terminal domains, respectively.