Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.
Proc Natl Acad Sci U S A
; 113(13): 3633-8, 2016 Mar 29.
Article
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| MEDLINE
| ID: mdl-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 α3ß3γ 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.
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1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
ATPasas de Translocación de Protón
/
Sistemas de Secreción Tipo III
Idioma:
En
Año:
2016
Tipo del documento:
Article