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Publication Abstract from PubMed

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. Paenibacillus 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.

Cryo-EM Structure of the Flagellar Motor Complex from Paenibacillus sp. TCA20.,Onoe S, Nishikino T, Kinoshita M, Takekawa N, Minamino T, Imada K, Namba K, Kishikawa JI, Kato T Biomolecules. 2025 Mar 18;15(3):435. doi: 10.3390/biom15030435. PMID:40149971^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.