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| Natura: | Artículo científico |
| Lingua: | en |
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Proceedings of the National Academy of Sciences of the United States of America
2025
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| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/39793043/ |
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| _version_ | 1868266258136301569 |
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| author | Nishikino, Tatsuro Takekawa, Norihiro Kishikawa, Jun-Ichi Hirose, Mika Kojima, Seiji Homma, Michio Kato, Takayuki Imada, Katsumi |
| author_facet | Nishikino, Tatsuro Takekawa, Norihiro Kishikawa, Jun-Ichi Hirose, Mika Kojima, Seiji Homma, Michio Kato, Takayuki Imada, Katsumi Nishikino, Tatsuro Takekawa, Norihiro Kishikawa, Jun-Ichi Hirose, Mika Kojima, Seiji Homma, Michio Kato, Takayuki Imada, Katsumi |
| collection | PubMed - marine biology |
| contents | Structural insight into sodium ion pathway in the bacterial flagellar stator from marine . Nishikino, Tatsuro Takekawa, Norihiro Kishikawa, Jun-Ichi Hirose, Mika Kojima, Seiji Homma, Michio Kato, Takayuki Imada, Katsumi Flagella Sodium Bacterial Proteins Cryoelectron Microscopy Vibrio Ions Models, Molecular Many bacteria swim in liquid or swarm on surface using the flagellum rotated by a motor driven by specific ion flow. The motor consists of the rotor and stator, and the stator converts the energy of ion flow to mechanical rotation. However, the ion pathway and the mechanism of stator rotation coupled with specific ion flow are still obscure. Here, we determined the structures of the sodium-driven stator of , namely PomAB, in the presence and absence of sodium ions and the structure with its specific inhibitor, phenamil, by cryo-electron microscopy. The structures and following functional analysis revealed the sodium ion pathway, the mechanism of ion selectivity, and the inhibition mechanism by phenamil. We propose a model of sodium ion flow coupled with the stator rotation based on the structures. This work provides insights into the molecular mechanisms of ion specificity and conversion of the electrochemical potential into mechanical functions. |
| format | Artículo científico |
| id | pubmed_39793043 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Proceedings of the National Academy of Sciences of the United States of America |
| record_format | pubmed |
| spellingShingle | Structural insight into sodium ion pathway in the bacterial flagellar stator from marine . Nishikino, Tatsuro Takekawa, Norihiro Kishikawa, Jun-Ichi Hirose, Mika Kojima, Seiji Homma, Michio Kato, Takayuki Imada, Katsumi Flagella Sodium Bacterial Proteins Cryoelectron Microscopy Vibrio Ions Models, Molecular Structural insight into sodium ion pathway in the bacterial flagellar stator from marine . Nishikino, Tatsuro Takekawa, Norihiro Kishikawa, Jun-Ichi Hirose, Mika Kojima, Seiji Homma, Michio Kato, Takayuki Imada, Katsumi Flagella Sodium Bacterial Proteins Cryoelectron Microscopy Vibrio Ions Models, Molecular Many bacteria swim in liquid or swarm on surface using the flagellum rotated by a motor driven by specific ion flow. The motor consists of the rotor and stator, and the stator converts the energy of ion flow to mechanical rotation. However, the ion pathway and the mechanism of stator rotation coupled with specific ion flow are still obscure. Here, we determined the structures of the sodium-driven stator of , namely PomAB, in the presence and absence of sodium ions and the structure with its specific inhibitor, phenamil, by cryo-electron microscopy. The structures and following functional analysis revealed the sodium ion pathway, the mechanism of ion selectivity, and the inhibition mechanism by phenamil. We propose a model of sodium ion flow coupled with the stator rotation based on the structures. This work provides insights into the molecular mechanisms of ion specificity and conversion of the electrochemical potential into mechanical functions. |
| title | Structural insight into sodium ion pathway in the bacterial flagellar stator from marine . |
| topic | Flagella Sodium Bacterial Proteins Cryoelectron Microscopy Vibrio Ions Models, Molecular |
| url | https://pubmed.ncbi.nlm.nih.gov/39793043/ |