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TitleIn situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque.
Journal, issue, pagesNat Microbiol, Vol. 10, Issue 7, Page 1723-1740, Year 2025
Publish dateJul 1, 2025
AuthorsTina Drobnič / Eli J Cohen / Thomas Calcraft / Mona Alzheimer / Kathrin Froschauer / Sarah Svensson / William H Hoffmann / Nanki Singh / Sriram G Garg / Louie D Henderson / Trishant R Umrekar / Andrea Nans / Deborah Ribardo / Francesco Pedaci / Ashley L Nord / Georg K A Hochberg / David R Hendrixson / Cynthia M Sharma / Peter B Rosenthal / Morgan Beeby /
PubMed AbstractThe bacterial flagellar motor, which spins a helical propeller for propulsion, has undergone evolutionary diversification across bacterial species, often involving the addition of structures ...The bacterial flagellar motor, which spins a helical propeller for propulsion, has undergone evolutionary diversification across bacterial species, often involving the addition of structures associated with increasing torque for motility in viscous environments. Understanding how such structures function and have evolved is hampered by challenges in visualizing motors in situ. Here we developed a Campylobacter jejuni minicell system for in situ cryogenic electron microscopy imaging and single-particle analysis of its motor, one of the most complex flagellar motors known, to subnanometre resolution. Focusing on the large periplasmic structures which are essential for increasing torque, our structural data, interpreted with molecular models, show that the basal disk comprises concentric rings of FlgP. The medial disk is a lattice of PflC with PflD, while the proximal disk is a rim of PflB attached to spokes of PflA. PflAB dimerization is essential for proximal disk assembly, recruiting FliL to scaffold more stator complexes at a wider radius which increases torque. We also acquired insights into universal principles of flagellar torque generation. This in situ approach is broadly applicable to other membrane-residing bacterial molecular machines.
External linksNat Microbiol / PubMed:40595286 / PubMed Central
MethodsEM (single particle) / EM (subtomogram averaging)
Resolution7.9 - 81.0 Å
Structure data

EMDB-16723: Wild-type Campylobacter jejuni flagellar motor, in situ
Method: EM (single particle) / Resolution: 9.36 Å

16724

9hmf

EMDB-16724: Periplasmic scaffold of the Campylobacter jejuni flagellar motor
PDB-9hmf: Periplasmic scaffold of the Campylobacter jejuni flagellar motor (alpha carbon trace)
Method: EM (single particle) / Resolution: 7.9 Å

EMDB-17415: Campylobacter jejuni flagellar motor, pflC deletion
Method: EM (subtomogram averaging) / Resolution: 80.0 Å

EMDB-17416: Campylobacter jejuni flagellar motor, pflD deletion
Method: EM (subtomogram averaging) / Resolution: 58.0 Å

EMDB-17417: Campylobacter jejuni flagellar motor, truncated PflA (d16-168)
Method: EM (subtomogram averaging) / Resolution: 57.5 Å

EMDB-17419: Campylobacter jejuni flagellar motor, FlgQ-mCherry fusion
Method: EM (subtomogram averaging) / Resolution: 81.0 Å

Source
  • campylobacter jejuni (Campylobacter)
KeywordsSTRUCTURAL PROTEIN / molecular machines / flagellar motor / molecular evolution / in situ / scaffold / MOTOR PROTEIN

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