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-Structure paper
タイトル | Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 4223, Year 2021 |
掲載日 | 2021年7月9日 |
著者 | Akihiro Kawamoto / Tomoko Miyata / Fumiaki Makino / Miki Kinoshita / Tohru Minamino / Katsumi Imada / Takayuki Kato / Keiichi Namba / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:34244518 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 - 11.6 Å |
構造データ | EMDB-30360: EMDB-30361: EMDB-30363: EMDB-30612, PDB-7d84: EMDB-30613: EMDB-30940: EMDB-30941: EMDB-30942: |
由来 |
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キーワード | MEMBRANE PROTEIN / Flagellar motor / Type III protein export system / Transmembrane protein Complex / Torque generation |