Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20
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 a...
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MDPI AG
2025-03-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/15/3/435 |
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| author | Sakura Onoe Tatsuro Nishikino Miki Kinoshita Norihiro Takekawa Tohru Minamino Katsumi Imada Keiichi Namba Jun-ichi Kishikawa Takayuki Kato |
| author_facet | Sakura Onoe Tatsuro Nishikino Miki Kinoshita Norihiro Takekawa Tohru Minamino Katsumi Imada Keiichi Namba Jun-ichi Kishikawa Takayuki Kato |
| author_sort | Sakura Onoe |
| collection | DOAJ |
| description | 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. <i>Paenibacillus</i> 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. |
| format | Article |
| id | doaj-art-cefc05e80da545bd91ae5fc63b8575b0 |
| institution | DOAJ |
| issn | 2218-273X |
| language | English |
| publishDate | 2025-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj-art-cefc05e80da545bd91ae5fc63b8575b02025-08-20T02:42:35ZengMDPI AGBiomolecules2218-273X2025-03-0115343510.3390/biom15030435Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20Sakura Onoe0Tatsuro Nishikino1Miki Kinoshita2Norihiro Takekawa3Tohru Minamino4Katsumi Imada5Keiichi Namba6Jun-ichi Kishikawa7Takayuki Kato8Institute for Protein Research, Osaka University, Suita 565-0871, Osaka, JapanInstitute for Protein Research, Osaka University, Suita 565-0871, Osaka, JapanGraduate School of Frontier Biosciences, Osaka University, Suita 565-0871, Osaka, JapanDepartment of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka 560-0043, Osaka, JapanGraduate School of Frontier Biosciences, Osaka University, Suita 565-0871, Osaka, JapanDepartment of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka 560-0043, Osaka, JapanGraduate School of Frontier Biosciences, Osaka University, Suita 565-0871, Osaka, JapanInstitute for Protein Research, Osaka University, Suita 565-0871, Osaka, JapanInstitute for Protein Research, Osaka University, Suita 565-0871, Osaka, JapanThe 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. <i>Paenibacillus</i> 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.https://www.mdpi.com/2218-273X/15/3/435flagella motorMotA1/MotB1 complexcryo-EMSPAstator complexantibiotics |
| spellingShingle | Sakura Onoe Tatsuro Nishikino Miki Kinoshita Norihiro Takekawa Tohru Minamino Katsumi Imada Keiichi Namba Jun-ichi Kishikawa Takayuki Kato Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20 Biomolecules flagella motor MotA1/MotB1 complex cryo-EM SPA stator complex antibiotics |
| title | Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20 |
| title_full | Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20 |
| title_fullStr | Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20 |
| title_full_unstemmed | Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20 |
| title_short | Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20 |
| title_sort | cryo em structure of the flagellar motor complex from i paenibacillus i sp tca20 |
| topic | flagella motor MotA1/MotB1 complex cryo-EM SPA stator complex antibiotics |
| url | https://www.mdpi.com/2218-273X/15/3/435 |
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