Abstract
We obtained a three-dimensional reconstruction of the flagellar filament of
Caulobacter crescentus CB15 from electron micrographs of negatively stained preparations. The
C. crescentus filament appears, both in negative stain and in the frozen-hydrated state, significantly smoother and narrower than other filaments. Its helical symmetry, and unit cell size, however, are similar to that of other filaments. Although the molecular weight of the
C. crescentus flagellin is about half that of other plain flagellins, there is only one monomer per unit cell as indicated by diffraction studies and by linear mass density measurements with the scanning transmission electron microscope. Alignment of the primary amino acid sequences of
Salmonella typhimurium (serotype i) and
C. crescentus (29,000
M
r) flagellins shows that whereas there is homology at the amino and carboxy-terminal ends of the two sequences, the central segment of the
S. typhimurium sequence has no homology to that of
C. crescentus. A correlated comparison between the three-dimensional reconstructions of the two filaments and primary amino acid sequences of the two flagellins suggests that: (1) the
C. crescentus subunit is missing the outer molecular domain but is, otherwise, similar to that of
S. typhimurium; (2) the outer molecular domain in
S. typhimurium corresponds, therefore, to a central stretch of the primary amino acid sequence; and (3) the outer molecular domain, missing in
C. crescentus, is not obligatory for flagellar motility.