Crystal structure of the FliF-FliG complex from Helicobacter pylori yields insight into the assembly of the motor MS-C ring in the bacterial flagellum.

ABSTRACT: The bacterial flagellar motor is a self-assembling supramolecular nanodevice. Its spontaneous biosynthesis is initiated by the insertion of the MS ring protein FliF into the inner membrane, followed by attachment of the switch protein FliG. Assembly of this multiprotein complex is tightly regulated to avoid nonspecific aggregation, but the molecular mechanisms governing flagellar assembly are unclear. Here, we present the crystal structure of the cytoplasmic domain of FliF complexed with the N-terminal domain of FliG (FliF _C -FliG _N ) from the bacterium Helicobacter pylori Within this complex, FliF _C interacted with FliG _N through extensive hydrophobic contacts similar to those observed in the FliF _C

SUBMITTER: Xue C 

PROVIDER: S-EPMC5808767 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature