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TitleMolecular architecture of the bacterial flagellar motor in cells.
Journal, issue, pagesBiochemistry, Vol. 53, Issue 27, Page 4323-4333, Year 2014
Publish dateJul 15, 2014
AuthorsXiaowei Zhao / Steven J Norris / Jun Liu /
PubMed AbstractThe flagellum is one of the most sophisticated self-assembling molecular machines in bacteria. Powered by the proton-motive force, the flagellum rapidly rotates in either a clockwise or ...The flagellum is one of the most sophisticated self-assembling molecular machines in bacteria. Powered by the proton-motive force, the flagellum rapidly rotates in either a clockwise or counterclockwise direction, which ultimately controls bacterial motility and behavior. Escherichia coli and Salmonella enterica have served as important model systems for extensive genetic, biochemical, and structural analysis of the flagellum, providing unparalleled insights into its structure, function, and gene regulation. Despite these advances, our understanding of flagellar assembly and rotational mechanisms remains incomplete, in part because of the limited structural information available regarding the intact rotor-stator complex and secretion apparatus. Cryo-electron tomography (cryo-ET) has become a valuable imaging technique capable of visualizing the intact flagellar motor in cells at molecular resolution. Because the resolution that can be achieved by cryo-ET with large bacteria (such as E. coli and S. enterica) is limited, analysis of small-diameter bacteria (including Borrelia burgdorferi and Campylobacter jejuni) can provide additional insights into the in situ structure of the flagellar motor and other cellular components. This review is focused on the application of cryo-ET, in combination with genetic and biophysical approaches, to the study of flagellar structures and its potential for improving the understanding of rotor-stator interactions, the rotational switching mechanism, and the secretion and assembly of flagellar components.
External linksBiochemistry / PubMed:24697492 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution33.0 - 41.0 Å
Structure data

EMDB-5912:
Cryo-electron tomography map of Leptospira interrogans flagellar motor
Method: EM (subtomogram averaging) / Resolution: 41.0 Å

EMDB-5913:
Cryo-electron tomography map of Leptospira interrogans flagellar motor with 16-fold symmetry imposed
Method: EM (subtomogram averaging) / Resolution: 33.0 Å

EMDB-5914:
Flagellar motor of Leptospira interrogans reconstructed by asymmetric reconstruction method
Method: EM (subtomogram averaging) / Resolution: 41.0 Å

Source
  • Leptospira interrogans (bacteria)

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