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PDBsum entry 5b0o

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Hydrolase/motor protein PDB id
5b0o
Contents
Protein chains
445 a.a.
(+ 0 more) 135 a.a.
126 a.a.
127 a.a.
Ligands
ADP ×4

References listed in PDB file
Key reference
Title Insight into the flagella type III export revealed by the complex structure of the type III atpase and its regulator.
Authors K.Imada, T.Minamino, Y.Uchida, M.Kinoshita, K.Namba.
Ref. Proc Natl Acad Sci U S A, 2016, 113, 3633-3638. [DOI no: 10.1073/pnas.1524025113]
PubMed id 26984495
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. 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.
Secondary reference #1
Title Crystallization and preliminary X-Ray analysis of the flih-Flii complex responsible for bacterial flagellar type III protein export.
Authors Y.Uchida, T.Minamino, K.Namba, K.Imada.
Ref. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012, 68, 1311-1314. [DOI no: 10.1107/S1744309112030801]
PubMed id 23143238
Abstract
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