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TitleMolecular model of a bacterial flagellar motor reveals a "parts-list" of protein adaptations to increase torque.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateOct 9, 2024
AuthorsTina Drobnič / Eli J Cohen / Tom Calcraft / Mona Alzheimer / Kathrin Froschauer / Sarah Svensson / William H Hoffmann / Nanki Singh / Sriram G Garg / Louie 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 AbstractOne hurdle to understanding how molecular machines work, and how they evolve, is our inability to see their structures . Here we describe a minicell system that enables cryogenic electron microscopy ...One hurdle to understanding how molecular machines work, and how they evolve, is our inability to see their structures . Here we describe a minicell system that enables cryogenic electron microscopy imaging and single particle analysis to investigate the structure of an iconic molecular machine, the bacterial flagellar motor, which spins a helical propeller for propulsion. We determine the structure of the high-torque motor including the subnanometre-resolution structure of the periplasmic scaffold, an adaptation essential to high torque. Our structure enables identification of new proteins, and interpretation with molecular models highlights origins of new components, reveals modifications of the conserved motor core, and explain how these structures both template a wider ring of motor proteins, and buttress the motor during swimming reversals. We also acquire insights into universal principles of flagellar torque generation. This approach is broadly applicable to other membrane-residing bacterial molecular machines complexes.
External linksbioRxiv / PubMed:39416179 / 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

EMDB-16724: Periplasmic scaffold of the Campylobacter jejuni flagellar motor
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

EMDB-19642: Campylobacter jejuni bacterial flagellar C-ring
Method: EM (subtomogram averaging) / Resolution: 20.0 Å

Source
  • Campylobacter jejuni (Campylobacter)

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