Proteopedia:Featured JRN/1

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Image:Anim Samatey2 FigA I.gif
Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.

Hideyuki Matsunami, Young-Ho Yoon, Vladimir Meshcheryakov, Keiichi Namba, and Fadel A. Samatey
Scientific Reports 6:27399 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. The mechanism of chaperone-mediated P-ring formation is poorly understood. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

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