7CGO

Cryo-EM structure of the flagellar motor-hook complex from Salmonella

This is a non-PDB format compatible entry.

Summary for 7CGO

• Entry DOI: 10.2210/pdb7cgo/pdb
• EMDB information: 30359
• Descriptor: Flagellar basal-body rod protein FlgG, Flagellar biosynthetic protein FliQ, Flagellar biosynthetic protein FliP, ... (16 entities in total)
• Functional Keywords: flagella, hook-basal body, motor protein
• Biological source: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720); More
• Total number of polymer chains: 219
• Total formula weight: 7785661.44

Authors

Tan, J.X.,Chang, S.H.,Wang, X.F.,Xu, C.H.,Zhou, Y.,Zhang, X.,Zhu, Y.Q. (deposition date: 2020-07-01, release date: 2021-04-28, Last modification date: 2021-05-26)

Primary citation

Tan, J.,Zhang, X.,Wang, X.,Xu, C.,Chang, S.,Wu, H.,Wang, T.,Liang, H.,Gao, H.,Zhou, Y.,Zhu, Y.
Structural basis of assembly and torque transmission of the bacterial flagellar motor.
Cell, 184:2665-2679.e19, 2021

PubMed Abstract: 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 cryoelectron 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.

PubMed: 33882274
DOI: 10.1016/j.cell.2021.03.057

Experimental method

ELECTRON MICROSCOPY (3.9 Å)