3AJW: Structure Of Flij, A Soluble Component Of Flagellar Type Iii Export Apparatus

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.
PDB ID: 3AJWDownload
MMDB ID: 88313
PDB Deposition Date: 2010/6/23
Updated in MMDB: 2011/05
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 3AJW: dimeric; determined by software (PISA)
Molecular Components in 3AJW
Label Count Molecule
Proteins (2 molecules)
Flagellar Flij Protein(Gene symbol: fliJ)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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