Journal
ELIFE
Volume 9, Issue -, Pages -Publisher
eLIFE SCIENCES PUBL LTD
DOI: 10.7554/eLife.53672
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Funding
- National Institutes of Health [R01 GM 110530, U01 AI 088752, R01 TW009504, R01 AI052473, R0 AI121207]
- Agencia Nacional de Investigacion e Innovacion [FCE_3_2016_1_126797, ALI_1_2014_1_4982, ANR-18-CE15-0027-1]
- Agence Nationale de la Recherche [ANR-18-CE15-0027-1, ANR-08-MIE-018]
- Pasteur International Joint Research Unit Integrative Microbiology of Zoonotic Agents (IMiZA)
- Institut Pasteur
- Agence Nationale de la Recherche (ANR) [ANR-18-CE15-0027] Funding Source: Agence Nationale de la Recherche (ANR)
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Spirochete bacteria, including important pathogens, exhibit a distinctive means of swimming via undulations of the entire cell. Motility is powered by the rotation of supercoiled 'endoflagella' that wrap around the cell body, confined within the periplasmic space. To investigate the structural basis of flagellar supercoiling, which is critical for motility, we determined the structure of native flagellar filaments from the spirochete Leptospira by integrating high-resolution cryo-electron tomography and X-ray crystallography. We show that these filaments are coated by a highly asymmetric, multi-component sheath layer, contrasting with flagellin-only homopolymers previously observed in exoflagellated bacteria. Distinct sheath proteins localize to the filament inner and outer curvatures to define the supercoiling geometry, explaining a key functional attribute of this spirochete flagellum.
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