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TitleStructural basis of assembly and torque transmission of the bacterial flagellar motor.
Journal, issue, pagesCell, Vol. 184, Issue 10, Page 2665-2679.e19, Year 2021
Publish dateMay 13, 2021
AuthorsJiaxing Tan / Xing Zhang / Xiaofei Wang / Caihuang Xu / Shenghai Chang / Hangjun Wu / Ting Wang / Huihui Liang / Haichun Gao / Yan Zhou / Yongqun Zhu /
PubMed AbstractThe 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 ...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.
External linksCell / PubMed:33882274
MethodsEM (single particle)
Resolution2.8 - 4.5 Å
Structure data

EMDB-30335, PDB-7cbl:
Cryo-EM structure of the flagellar LP ring from Salmonella
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-30336, PDB-7cbm:
Cryo-EM structure of the flagellar distal rod with partial hook from Salmonella
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-30348, PDB-7cg0:
Cryo-EM structure of the flagellar proximal rod with FliF peptides from Salmonella
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-30350, PDB-7cg4:
Cryo-EM structure of the flagellar export apparatus with FliE from Salmonella
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-30351, PDB-7cg7:
Cryo-EM structure of the flagellar MS ring with C34 symmetry from Salmonella
Method: EM (single particle) / Resolution: 3.61 Å

EMDB-30354, PDB-7cgb:
Cryo-EM structure of the flagellar hook from Salmonella
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-30359, PDB-7cgo:
Cryo-EM structure of the flagellar motor-hook complex from Salmonella
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-31006, PDB-7e80:
Cryo-EM structure of the flagellar rod with hook and export apparatus from Salmonella
Method: EM (single particle) / Resolution: 3.67 Å

EMDB-31007, PDB-7e81:
Cryo-EM structure of the flagellar MS ring with FlgB-Dc loop and FliE-helix 1 from Salmonella
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-31008, PDB-7e82:
Cryo-EM structure of the flagellar rod with partial hook from Salmonella
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-OCA:
OCTANOIC ACID (CAPRYLIC ACID)

Source
  • salmonella typhimurium (strain lt2 / sgsc1412 / atcc 700720) (bacteria)
  • Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
KeywordsMOTOR PROTEIN / Flagella / LP ring / FlgH / FlgI / Distal rod / FlgG / FlgF / Proximal rod / FlgC / FlgB / FliF / Export apparatus / FliE / MS ring / Hook / FlgE / Hook-basal body / Rod / Motor-hook

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