{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Imada K"],"funding":["Ministry of Education, Culture, Sports, Science, and Technology","Japan Society for the Promotion of Science"],"pagination":["3633-8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4822572"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["113(13)"],"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 o"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator."],"pmcid":["PMC4822572"],"funding_grant_id":["15H01640","23115008","21227006","15H02386","24117004","25121718","25000013","26293097"],"pubmed_authors":["Minamino T","Kinoshita M","Imada K","Uchida Y","Namba K"],"additional_accession":[]},"is_claimable":false,"name":"Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.","description":"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 o","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Mar","modification":"2025-04-04T12:38:49.61Z","creation":"2019-03-27T03:11:20Z"},"accession":"S-EPMC4822572","cross_references":{"pubmed":["26984495"],"doi":["10.1073/pnas.1524025113"]}}