The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo

Sci Rep. 2019 Oct 18;9(1):14948. doi: 10.1038/s41598-019-51440-1.

Abstract

Bacteria swim and swarm by rotating the micrometers long, helical filaments of their flagella. They change direction by reversing their flagellar rotation, which switches the handedness of the filament's supercoil. So far, all studied functional filaments are composed of a mixture of L- and R-state flagellin monomers. Here we show in a study of the wild type Firmicute Kurthia sp., that curved, functional filaments can adopt a conformation in vivo that is closely related to a uniform, all-L-state. This sheds additional light on transitions of the flagellar supercoil and uniquely reveals the atomic structure of a wild-type flagellar filament in vivo, including six residues showing clearly densities of O-linked glycosylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anisotropy
  • Bacterial Proteins / chemistry
  • Cryoelectron Microscopy
  • Firmicutes / physiology*
  • Flagella / physiology*
  • Flagella / ultrastructure
  • Flagellin / chemistry
  • Fourier Analysis
  • Glycosylation
  • Planococcaceae / physiology*
  • Software

Substances

  • Bacterial Proteins
  • Flagellin