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9LUB

The chimeric flagellar motor complex between MotA1B1 from Paenibacillus sp. TCA20 and MotAB from E.coli, state 2

Summary for 9LUB
Entry DOI10.2210/pdb9lub/pdb
EMDB information63393
DescriptorFlagellar 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 Keywordsflagellar, motility, paenibacillus, motor protein
Biological sourcePaenibacillus sp. TCA20
More
Total number of polymer chains7
Total formula weight213365.69
Authors
Onoe, S.,Nishikino, T.,Kinoshita, M.,Kishikawa, J.,Kato, T. (deposition date: 2025-02-08, release date: 2025-04-09)
Primary citationOnoe, 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: 40149971
DOI: 10.3390/biom15030435
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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PDB entries from 2025-05-28

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