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-Structure paper
| タイトル | Cryo-EM Structure of the Flagellar Motor Complex from sp. TCA20. |
|---|---|
| ジャーナル・号・ページ | Biomolecules, Vol. 15, Issue 3, Year 2025 |
| 掲載日 | 2025年3月18日 |
著者 | Sakura Onoe / Tatsuro Nishikino / Miki Kinoshita / Norihiro Takekawa / Tohru Minamino / Katsumi Imada / Keiichi Namba / Jun-Ichi Kishikawa / Takayuki Kato / ![]() |
| PubMed 要旨 | The bacterial flagellum, a complex nanomachine composed of numerous proteins, is utilized by bacteria for swimming in various environments and plays a crucial role in their survival and infection. ...The bacterial flagellum, a complex nanomachine composed of numerous proteins, is utilized by bacteria for swimming in various environments and plays a crucial role in their survival and infection. The flagellar motor is composed of a rotor and stator complexes, with each stator unit functioning as an ion channel that converts flow from outside of cell membrane into rotational motion. sp. TCA20 was discovered in a hot spring, and a structural analysis was conducted on the stator complex using cryo-electron microscopy to elucidate its function. Two of the three structures (Classes 1 and 3) were found to have structural properties typical for other stator complexes. In contrast, in Class 2 structures, the pentamer ring of the A subunits forms a C-shape, with lauryl maltose neopentyl glycol (LMNG) bound to the periplasmic side of the interface between the A and B subunits. This interface is conserved in all stator complexes, suggesting that hydrophobic ligands and lipids can bind to this interface, a feature that could potentially be utilized in the development of novel antibiotics aimed at regulating cell motility and infection. |
リンク | Biomolecules / PubMed:40149971 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.3 - 3.5 Å |
| 構造データ | EMDB-63392, PDB-9lu9: EMDB-63393, PDB-9lub: EMDB-63394, PDB-9luc: |
| 化合物 | ![]() ChemComp-AV0: |
| 由来 |
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キーワード | MOTOR PROTEIN / Flagellar / motility / Paenibacillus |
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paenibacillus sp. tca20 (バクテリア)
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