Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex.

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dc.contributor.authorQin, Zhuan
dc.contributor.authorTu, Jiagang
dc.contributor.authorLin, Tao
dc.contributor.authorNorris, Steven J.
dc.contributor.authorLi, Chunhao
dc.contributor.authorMotaleb, Md A.
dc.date.accessioned2020-04-28T16:10:40Z
dc.date.available2020-04-28T16:10:40Z
dc.date.issued2018-11-09
dc.description.abstractPeriplasmic flagella are essential for the distinct morphology and motility of spirochetes. A flagella-specific type III secretion system (fT3SS) composed of a membrane-bound export apparatus and a cytosolic ATPase complex is responsible for the assembly of the periplasmic flagella. Here, we deployed cryo-electron tomography (cryo-ET) to visualize the fT3SS machine in the Lyme disease spirochete Borrelia burgdorferi. We show, for the first time, that the cytosolic ATPase complex is attached to the flagellar C-ring through multiple spokes to form the “spoke and hub” structure in B. burgdorferi. This structure not only strengthens structural rigidity of the round-shaped C-ring but also appears to rotate with the C-ring. Our studies provide structural insights into the unique mechanisms underlying assembly and rotation of the periplasmic flagella and may provide the basis for the development of novel therapeutic strategies against several pathogenic spirochetes.en_US
dc.identifier.doi10.1371/journal.pbio.3000050
dc.identifier.urihttp://hdl.handle.net/10342/8433
dc.titleCryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex.en_US
dc.typeArticleen_US
ecu.journal.issue11en_US
ecu.journal.namePLoS Biologyen_US
ecu.journal.pagese3000050en_US
ecu.journal.volume16en_US

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