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TitleAn asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateMar 11, 2020
AuthorsKimberley H Gibson / Felipe Trajtenberg / Elsio A Wunder / Megan R Brady / Fabiana San Martin / Ariel Mechaly / Zhiguo Shang / Jun Liu / Mathieu Picardeau / Albert Ko / Alejandro Buschiazzo / Charles Vaughn Sindelar /
PubMed AbstractSpirochete 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 ...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 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.
External linksElife / PubMed:32157997 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution9.83 - 18.4 Å
Structure data

EMDB-20503:
Subtomogram average of a purified Leptospira biflexa -fcpB mutant flagellum
Method: EM (subtomogram averaging) / Resolution: 18.4 Å

20504

6pwb

EMDB-20504: 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging
PDB-6pwb: Rigid body fitting of flagellin FlaB, and flagellar coiling proteins, FcpA and FcpB, into a 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging
Method: EM (subtomogram averaging) / Resolution: 9.83 Å

Source
  • Leptospira biflexa serovar Patoc (bacteria)
  • Leptospira biflexa serovar Patoc strain 'Patoc 1 (Paris)' (bacteria)
  • leptospira biflexa serovar patoc (strain patoc 1 / atcc 23582 / paris) (bacteria)
KeywordsSTRUCTURAL PROTEIN / bacterial flagella / FcpA / FcpB / FlaA / FlaB / Leptospira

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