3ajw | pdb_00003ajw

Structure of FliJ, a soluble component of flagellar type III export apparatus

spinqualitylabelsall models 3ajw, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ajw is a 1 chain structure with sequence from "bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FLIJ_SALTY] Flagellar protein that affects chemotactic events. Publication Abstract from PubMed The proteins that form the bacterial flagellum are translocated to its distal end through the central channel of the growing flagellum by the flagellar-specific protein export apparatus, a family of the type III protein secretion system. FliI and FliJ are soluble components of this apparatus. FliI is an ATPase that has extensive structural similarity to the alpha and beta subunits of F(o)F(1)-ATP synthase. FliJ is essential for export, but its function remains obscure. Here we show that the structure of FliJ derived from Salmonella enterica serovar Typhimurium is remarkably similar to that of the two-stranded alpha-helical coiled-coil part of the gamma subunit of F(o)F(1)-ATP synthase and that FliJ promotes the formation of FliI hexamer rings by binding to the center of the ring. These results suggest that the type III protein export system and F- and V-type ATPases share a similar mechanism and an evolutionary relationship. Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases.,Ibuki T, Imada K, Minamino T, Kato T, Miyata T, Namba K Nat Struct Mol Biol. 2011 Mar;18(3):277-82. Epub 2011 Jan 30. PMID:21278755 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flagellar protein 3D structures

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