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- W2092305456 abstract "Bacterial motility is achieved by rotation of flagella. The bacterial flagellum is a macromolecular complex that allows bacterial cells to swim in liquid environment. The complex is composed of the helical filament, the flexible hook and the basal body embedded in bacterial inner and outer membranes penetrating peptidoglycan layer. The basal body is divided into three sub-structures, the LP-ring, the MS-ring and the rod. The LP-ring, as molecular bushing, spans between bacterial outer membrane and peptidoglycan layer. FlgH and FlgI are the subunit proteins of the LP-ring and a periplasmic flagellar protein FlgA is involved in the P-ring assembly. Previous biochemical studies indicated that FlgA might associate with FlgI after secretion into the periplasm and act as a key protein for the flagellar P-ring assembly. The atomic structure of Salmonella FlgA has been determined at 2.1 Å resolution. The over-all structure revealed that FlgA comprised of two distinct domains as previously shown by limited-proteolysis experiments. The beta-clip fold in the FlgA structure could be involve in binding to peptidoglycan. FlgA mediates the assembly of the flagellar P-ring by means of its interactions with the carbohydrate moieties of peptidoglycan. Site-directed mutagenesis to residues at the putative FlgI binding site of FlgA caused reduced ability to complement in the FlgA-deficient Salmonella strain, indicating that FlgI required the constitutive interaction with FlgA in the flagellar P-ring assembly. We discuss about fundamental functions of FlgA and propose the molecular mechanism of the flagellar P-ring assembly." @default.
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- W2092305456 date "2010-01-01" @default.
- W2092305456 modified "2023-09-26" @default.
- W2092305456 title "Crystal Structure and Mutational Analysis of the Periplasmic Flagellar Protein FlgA" @default.
- W2092305456 doi "https://doi.org/10.1016/j.bpj.2009.12.3034" @default.
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