title: Pairwise perturbation of flagellin subunits. The structural basis for the differences between plain and complex bacterial flagellar filaments.
abstract: Although plain and complex bacterial flagellar filaments differ in their physical properties and helical symmetry, they both appear to derive from a common underlying structure. Analysis of electron micrographs of complex filaments of Rhizobium lupini revealed that the unit cell has twice the length of that of plain filaments, with a corresponding reduction in helical symmetry whereby the six-start helical family present in plain filaments collapses into a three-start family. Mass per unit length measurements were made by scanning transmission electron microscopy. These, together with the unit cell dimensions and the molecular weight of the flagellin monomer, enabled the number of monomers per unit cell to be estimated. Whereas plain filaments have a single monomer per unit cell, complex filaments have two. These results suggest that complex filament structure differs from plain filament structure by a pairwise perturbation, or interaction, of the flagellin monomers. The additional bonding interactions involved in the perturbation in the complex filament may make it more rigid than the plain filament, which has no such perturbation.
mesh_terms: D001426:Bacterial Proteins; D005407:Flagella / Q000648:ultrastructure; D005408:Flagellin; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D012231:Rhizobium / Q000648:ultrastructure; D012486:Salmonella typhimurium / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins; D046911:Macromolecular Substances; D005408:Flagellin