9LUB
The chimeric flagellar motor complex between MotA1B1 from Paenibacillus sp. TCA20 and MotAB from E.coli, state 2
Summary for 9LUB
Entry DOI | 10.2210/pdb9lub/pdb |
EMDB information | 63393 |
Descriptor | Flagellar motor protein MotA, Chimeric B subunit of MotA1B1 from Paenibacillus sp. TCA20 and MotAB from E. coli,Motility protein B (2 entities in total) |
Functional Keywords | flagellar, motility, paenibacillus, motor protein |
Biological source | Paenibacillus sp. TCA20 More |
Total number of polymer chains | 7 |
Total formula weight | 213365.69 |
Authors | Onoe, S.,Nishikino, T.,Kinoshita, M.,Kishikawa, J.,Kato, T. (deposition date: 2025-02-08, release date: 2025-04-09) |
Primary citation | Onoe, S.,Nishikino, T.,Kinoshita, M.,Takekawa, N.,Minamino, T.,Imada, K.,Namba, K.,Kishikawa, J.I.,Kato, T. Cryo-EM Structure of the Flagellar Motor Complex from Paenibacillus sp. TCA20. Biomolecules, 15:-, 2025 Cited by PubMed Abstract: 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. PubMed: 40149971DOI: 10.3390/biom15030435 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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