Cryo-EM structure of the flagellar MS ring with FlgB-Dc loop and FliE-helix 1 from Salmonella (PDB ID: 7E81)

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Cryo-EM structure of the flagellar MS ring with FlgB-Dc loop and FliE-helix 1 from Salmonella (PDB ID: 7E81)

The bacterial flagellar motor is a supramolecular protein machine that drives rotation of the flagellum for motility, which is essential for bacterial survival in different environments and a key determinant of pathogenicity. The detailed structure of the flagellar motor remains unknown. Here we present an atomic-resolution cryo electron microscopy (cryo-EM) structure of the bacterial flagellar motor complexed with the hook, consisting of 175 subunits with a molecular mass of approximately 6.3 MDa. The structure reveals that 10 peptides protruding from the MS ring with the FlgB and FliE subunits mediate torque transmission from the MS ring to the rod and overcome the symmetry mismatch between the rotational and helical structures in the motor. The LP ring contacts the distal rod and applies electrostatic forces to support its rotation and torque transmission to the hook. This work provides detailed molecular insights into the structure, assembly, and torque transmission mechanisms of the flagellar motor. 

An illustration image of the protein structure rendered using 3D Protein Imaging (https://3dproteinimaging.com/about-protein-imager/) and Adobe Photoshop.

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