Structural similarity between the flagellar type III ATPase Flil and F1-ATPase subunits

Construction of the bacterial flagellum in the cell exterior proceeds at its distal end by highly ordered self-assembly of many different component proteins, which are selectively exported through the central channel of the growing flagellum by the flagellar type III export apparatus. Flil is the ATIPase of the export apparatus that drives the export process. Here we report the 2.4 angstrom resolution crystal structure of Fill in the ADP-bound form. Fill consists of three domains, and the whole structure shows extensive similarities to the alpha and beta subunits of F0F1-ATPsynthase, a rotary motor that drives the chemical reaction of ATIP synthesis. A hexamer model of Flil has been constructed based on the F0F1-ATPase structure composed of the alpha(3)beta(3)gamma subunits. Although the regions that differ in conformation between Flil and the F-1-alpha/beta subunits are all located on the outer surface of the hexamer ring, the main chain structures at the subunit interface and those surrounding the central channel of the ring are well conserved. These results imply an evolutionary relation between the flagellum and F0F1-ATPsynthase and a similarity in the mechanism between Flil and F-1-ATPase despite the apparently different functions of these proteins.