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. 2024 Sep 6;15(10):e01261-24. doi: 10.1128/mbio.01261-24

Fig 3.

3D structures of Vibrio FliF and several Salmonella FliF models. It depicts overall structures, side views highlighting structural angles, and detailed views of specific regions and amino acid interactions in the protein structures.

Comparison of the various S-ring and FliF structures. (A) Cross-section view of the Cα ribbon drawing of the S-ring structures from the MS-ring formed by Vibrio FliFG fusion protein (34-mer, this study), the intact flagellar hook basal body in Salmonella (PDB ID: 7CGO), the MS-ring formed by Salmonella FliF (PDB ID: 6SD3), and the MS-ring formed by Salmonella FliF (PDB ID: 7D84). All have 34-fold rotational symmetry. A protomer in each ring is colored in rainbow. (B) Comparison of FliF protomer structures in the S-rings. The protomers colored in rainbow in panel A are shown. The inclination angles of the RBM3, the antiparallel β2/β5 strands, or the β3/β4 strands relative to the horizontal are shown. (C and D) Comparison of the protruding triangular β2–β3 loops in Vibrio FliF (this study) and Salmonella FliF (PDB ID: 7D84) structures. Left: stick models of the main chains. Right: stick models with the side chains. The secondary structure elements are labeled with gray text in panels B–D.