2dpy
Crystal structure of the flagellar type III ATPase FliI
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OverviewOverview
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. FliI is, the ATPase of the export apparatus that drives the export process. Here we, report the 2.4 A resolution crystal structure of FliI in the ADP-bound, form. FliI 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 ATP synthesis. A, hexamer model of FliI has been constructed based on the F1-ATPase, structure composed of the alpha3beta3gamma subunits. Although the regions, that differ in conformation between FliI and the F1-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 FliI and F1-ATPase despite the, apparently different functions of these proteins.
About this StructureAbout this Structure
2DPY is a Single protein structure of sequence from Salmonella typhimurium with ADP as ligand. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
ReferenceReference
Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits., Imada K, Minamino T, Tahara A, Namba K, Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):485-90. Epub 2007 Jan 3. PMID:17202259
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