Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli.

Abstract excerpt

The FliG protein of Escherichia coli is essential for assembly and function of the flagellar motor. Certain mutations in FliG give a non-motile, or Mot-, phenotype, in which flagella are assembled but do not rotate. Mutations with this property are clustered in a C-terminal segment of FliG that is stable when expressed alone, and thus probably constitutes an independently folded domain. Previously, we suggested...

Topics

• Bacterial Proteins
• Binding Sites
• Conserved Sequence
• Escherichia coli
• Flagella
• Mutagenesis
• Mutation
• Phenotype
• Sequence Alignment