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TitleNative flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 4223, Year 2021
Publish dateJul 9, 2021
AuthorsAkihiro Kawamoto / Tomoko Miyata / Fumiaki Makino / Miki Kinoshita / Tohru Minamino / Katsumi Imada / Takayuki Kato / Keiichi Namba /
PubMed AbstractThe bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly. The C ring attached to the MS ring is involved in torque ...The bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly. The C ring attached to the MS ring is involved in torque generation and rotation switch, and a large symmetry mismatch between these two rings has been a long puzzle, especially with respect to their role in motor function. Here, using cryoEM structural analysis of the flagellar basal body and the MS ring formed by full-length FliF from Salmonella enterica, we show that the native MS ring is formed by 34 FliF subunits with no symmetry variation. Symmetry analysis of the C ring shows a variation with a peak at 34-fold, suggesting flexibility in C ring assembly. Finally, our data also indicate that FliF subunits assume two different conformations, contributing differentially to the inner and middle parts of the M ring and thus resulting in 23- and 11-fold subsymmetries in the inner and middle M ring, respectively. The internal core of the M ring, formed by 23 subunits, forms a hole of the right size to accommodate the protein export gate.
External linksNat Commun / PubMed:34244518 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 11.6 Å
Structure data

EMDB-30360:
34-fold symmetry salmonella MS ring
Method: EM (single particle) / Resolution: 7.5 Å

EMDB-30361:
11 fold-syymetry of salmonella MS ring
Method: EM (single particle) / Resolution: 8.9 Å

EMDB-30363:
Without imposing symmetry of salmonella MS ring
Method: EM (single particle) / Resolution: 11.6 Å

30612

7d84

EMDB-30612, PDB-7d84:
34-fold symmetry Salmonella S ring formed by full-length FliF
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-30613:
Structure of the bacterial flagellar basal body
Method: EM (single particle) / Resolution: 6.8 Å

EMDB-30940:
Salmonella flagella MS-ring protein FliF 1-503 having C33 symmetry
Method: EM (single particle) / Resolution: 6.9 Å

EMDB-30941:
Salmonella flagella MS-ring protein FliF 1-456 having C35 symmetry
Method: EM (single particle) / Resolution: 4.59 Å

EMDB-30942:
Salmonella flagella MS-ring protein FliF 1-456 having C34 symmetry
Method: EM (single particle) / Resolution: 4.46 Å

Source
  • Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
  • Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (bacteria)
  • salmonella enterica serovar typhimurium (bacteria)
KeywordsMEMBRANE PROTEIN / Flagellar motor / Type III protein export system / Transmembrane protein Complex / Torque generation

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