8th8

Linker domain of Nexin-dynein regulatory complex from Tetrahymena thermophilaLinker domain of Nexin-dynein regulatory complex from Tetrahymena thermophila

Structural highlights 8th8 is a 11 chain structure with sequence from Tetrahymena thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 7.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q229S1_TETTS Publication Abstract from PubMed 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. Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism.,Ghanaeian A, Majhi S, McCafferty CL, Nami B, Black CS, Yang SK, Legal T, Papoulas O, Janowska M, Valente-Paterno M, Marcotte EM, Wloga D, Bui KH Nat Commun. 2023 Sep 15;14(1):5741. doi: 10.1038/s41467-023-41480-7. PMID:37714832 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 8th8, resolution 7.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image