5b0o
From Proteopedia
Structure of the FliH-FliI complex
Structural highlights
FunctionFLII_SALTY Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum. May be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. Publication Abstract from PubMedFliI 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 alpha3beta3gamma 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. FliHC2shows 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. Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.,Imada K, Minamino T, Uchida Y, Kinoshita M, Namba K Proc Natl Acad Sci U S A. 2016 Mar 29;113(13):3633-8. doi:, 10.1073/pnas.1524025113. Epub 2016 Mar 16. PMID:26984495[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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