8TID

Combined linker domain of N-DRC and associated proteins Tetrahymena

This is a non-PDB format compatible entry.

Summary for 8TID

• Entry DOI: 10.2210/pdb8tid/pdb
• EMDB information: 41284 41376
• Descriptor: Dynein regulatory complex protein 1/2 N-terminal domain-containing protein, Dynein regulatory complex protein 9, Dynein regulatory complex protein 10, ... (24 entities in total)
• Functional Keywords: nexin-dynein regulatory complex, cilia, axoneme, dynein, structural protein
• Biological source: Tetrahymena thermophila; More
• Total number of polymer chains: 30
• Total formula weight: 2072904.54

Authors

Ghanaeian, A.G.,Majhi, S.M.,McCaffrey, C.M.,Nami, B.N.,Black, C.B.,Yang, S.K.,Legal, T.L.,Papoulas, O.P.,Janowska, M.J.,Valente-Paterno, M.V.,Marcotte, E.M.,Wloga, D.W.,Bui, K.H. (deposition date: 2023-07-19, release date: 2023-09-27, Last modification date: 2024-11-13)

Primary citation

Ghanaeian, A.,Majhi, S.,McCafferty, C.L.,Nami, B.,Black, C.S.,Yang, S.K.,Legal, T.,Papoulas, O.,Janowska, M.,Valente-Paterno, M.,Marcotte, E.M.,Wloga, D.,Bui, K.H.
Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism.
Nat Commun, 14:5741-5741, 2023

PubMed Abstract: Cilia are hairlike protrusions that project from the surface of eukaryotic cells and play key roles in cell signaling and motility. Ciliary motility is regulated by the conserved nexin-dynein regulatory complex (N-DRC), which links adjacent doublet microtubules and regulates and coordinates the activity of outer doublet complexes. Despite its critical role in cilia motility, the assembly and molecular basis of the regulatory mechanism are poorly understood. Here, using cryo-electron microscopy in conjunction with biochemical cross-linking and integrative modeling, we localize 12 DRC subunits in the N-DRC structure of Tetrahymena thermophila. We also find that the CCDC96/113 complex is in close contact with the DRC9/10 in the linker region. In addition, we reveal that the N-DRC is associated with a network of coiled-coil proteins that most likely mediates N-DRC regulatory activity.

PubMed: 37714832
DOI: 10.1038/s41467-023-41480-7

Experimental method

ELECTRON MICROSCOPY (3.6 Å)