EMD-30335
Cryo-EM structure of the flagellar LP ring from Salmonella
EMD-30335
Single-particle2.8 Å
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Map released: 28/04/2021
Last modified: 20/11/2024
Sample Organism:
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Sample: Flagellar hook-basal body
Fitted models: 7cbl (Avg. Q-score: 0.588)
Deposition Authors: Tan JX, Chang SH
Sample: Flagellar hook-basal body
Fitted models: 7cbl (Avg. Q-score: 0.588)
Deposition Authors: Tan JX, Chang SH
Structural basis of assembly and torque transmission of the bacterial flagellar motor.
Tan J,
Zhang X,
Wang X,
Xu C,
Chang S,
Wu H,
Wang T,
Liang H,
Gao H
,
Zhou Y,
Zhu Y
(2021) Cell , 184 , 2665 - 2679.e19
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(2021) Cell , 184 , 2665 - 2679.e19
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.
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.