5B0O

Structure of the FliH-FliI complex

Summary for 5B0O

• Entry DOI: 10.2210/pdb5b0o/pdb
• Related: 2DPY
• Descriptor: Flagellum-specific ATP synthase, Flagellar assembly protein FliH, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: bacterial flagellum, type iii secretion, atpase, peripheral stalk, hydrolase-motor protein complex, hydrolase/motor protein
• Biological source: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720); More
• Cellular location: Cytoplasm : P26465 P15934
• Total number of polymer chains: 12
• Total formula weight: 321670.54

Authors

Imada, K.,Uchida, Y.,Kinoshita, M.,Namba, K.,Minamino, T. (deposition date: 2015-11-02, release date: 2016-03-23, Last modification date: 2023-11-08)

Primary citation

Imada, K.,Minamino, T.,Uchida, Y.,Kinoshita, M.,Namba, K.
Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator
Proc.Natl.Acad.Sci.USA, 113:3633-3638, 2016

PubMed Abstract: FliI and FliJ form the FliI6FliJ ATPase complex of the bacterial flagellar export apparatus, a member of the type III secretion system. The FliI6FliJ complex is structurally similar to the α3β3γ complex of F1-ATPase. The FliH homodimer binds to FliI to connect the ATPase complex to the flagellar base, but the details are unknown. Here we report the structure of the homodimer of a C-terminal fragment of FliH (FliHC2) in complex with FliI. FliHC2 shows an unusually asymmetric homodimeric structure that markedly resembles the peripheral stalk of the A/V-type ATPases. The FliHC2-FliI hexamer model reveals that the C-terminal domains of the FliI ATPase face the cell membrane in a way similar to the F/A/V-type ATPases. We discuss the mechanism of flagellar ATPase complex formation and a common origin shared by the type III secretion system and the F/A/V-type ATPases.

PubMed: 26984495
DOI: 10.1073/pnas.1524025113

Experimental method

X-RAY DIFFRACTION (3 Å)