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9D2F

3D structure and atomic model of RS3 of mouse respiratory cilia

This is a non-PDB format compatible entry.
Summary for 9D2F
Entry DOI10.2210/pdb9d2f/pdb
EMDB information46494
DescriptorAdenylate kinase 9, Cilia- and flagella-associated protein 43, Cilia- and flagella-associated protein 44, ... (25 entities in total)
Functional Keywordsaxoneme, radial spoke, structural protein
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains29
Total formula weight3090152.63
Authors
Yanhe, Z.,Xuewu, Z.,Daniela, N. (deposition date: 2024-08-08, release date: 2025-08-13, Last modification date: 2026-02-25)
Primary citationZhao, Y.,Song, K.,Tavakoli, A.,Gui, L.,Fernandez-Gonzalez, A.,Zhang, S.,Dzeja, P.P.,Mitsialis, S.A.,Zhang, X.,Nicastro, D.
Mouse radial spoke 3 is a metabolic and regulatory hub in cilia.
Nat.Struct.Mol.Biol., 32:1542-1554, 2025
Cited by
PubMed Abstract: Cilia are microtubule-based organelles that have important roles in cell sensing, signaling and motility. Recent studies have revealed the atomic structures of many multicomponent ciliary complexes, elucidating their mechanisms of action. However, little is known about the structure, proteome and function of full-length radial spoke 3 (RS3), a conserved complex that transmits mechanochemical signals to coordinate ciliary motility. Here, we combined single-particle cryo-electron microscopy, cryo-electron tomography, proteomic analysis and computational modeling to determine the three-dimensional structure and atomic model of RS3 from mouse respiratory cilia. We reveal all RS3 components, including regulatory and metabolic enzymes such as a protein kinase A subunit, adenylate kinases (AKs) and malate dehydrogenases. Furthermore, we confirm RS3 loss in AK7-deficient mice, which exhibit motility defects. Our findings identify RS3 as an important regulatory and metabolic hub that maintains sufficient adenosine triphosphate for sustained ciliary beating, providing insights into the etiology of ciliopathies.
PubMed: 40579595
DOI: 10.1038/s41594-025-01594-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.7 Å)
Structure validation

250359

건을2026-03-11부터공개중

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