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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Main Authors: Sakura Onoe, Tatsuro Nishikino, Miki Kinoshita, Norihiro Takekawa, Tohru Minamino, Katsumi Imada, Keiichi Namba, Jun-ichi Kishikawa, Takayuki Kato
Format: Article
Language:English
Published: MDPI AG 2025-03-01
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.
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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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