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- PDB-8tid: Combined linker domain of N-DRC and associated proteins Tetrahymena -
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Open data
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Basic information
Entry | Database: PDB / ID: 8tid | |||||||||
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Title | Combined linker domain of N-DRC and associated proteins Tetrahymena | |||||||||
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![]() | STRUCTURAL PROTEIN / nexin-dynein regulatory complex / cilia / axoneme / dynein | |||||||||
Function / homology | ![]() regulation of cilium movement / axonemal dynein complex assembly / epithelial cilium movement involved in determination of left/right asymmetry / inner dynein arm assembly / sperm axoneme assembly / cytoskeletal motor regulator activity / sperm principal piece / cilium-dependent cell motility / axonemal dynein complex / regulation of cilium beat frequency involved in ciliary motility ...regulation of cilium movement / axonemal dynein complex assembly / epithelial cilium movement involved in determination of left/right asymmetry / inner dynein arm assembly / sperm axoneme assembly / cytoskeletal motor regulator activity / sperm principal piece / cilium-dependent cell motility / axonemal dynein complex / regulation of cilium beat frequency involved in ciliary motility / regulation of Arp2/3 complex-mediated actin nucleation / axoneme assembly / flagellated sperm motility / actomyosin structure organization / motile cilium / myosin II complex / locomotion / positive regulation of cell motility / myosin heavy chain binding / axoneme / mitotic cytokinesis / cilium assembly / sperm flagellum / ciliary basal body / post-embryonic development / cell projection / cell motility / cilium / small GTPase binding / cell migration / lamellipodium / microtubule binding / microtubule / cytoskeleton / calcium ion binding / Golgi apparatus / ATP hydrolysis activity / ATP binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
![]() | 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. ...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. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism. Authors: Avrin Ghanaeian / Sumita Majhi / Caitlyn L McCafferty / Babak Nami / Corbin S Black / Shun Kai Yang / Thibault Legal / Ophelia Papoulas / Martyna Janowska / Melissa Valente-Paterno / Edward ...Authors: Avrin Ghanaeian / Sumita Majhi / Caitlyn L McCafferty / Babak Nami / Corbin S Black / Shun Kai Yang / Thibault Legal / Ophelia Papoulas / Martyna Janowska / Melissa Valente-Paterno / Edward M Marcotte / Dorota Wloga / Khanh Huy Bui / ![]() ![]() ![]() 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 ...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. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.7 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 41284MC ![]() 8tekC ![]() 8th8C M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Dynein regulatory complex protein ... , 3 types, 3 molecules AJK
#1: Protein | Mass: 98840.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#10: Protein | Mass: 44990.227 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#11: Protein | Mass: 51315.023 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Coiled-coil protein, ... , 2 types, 3 molecules BOo
#2: Protein | Mass: 60596.348 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#15: Protein | Mass: 105196.055 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Protein , 15 types, 20 molecules CGHIiLMNnPQRSsUVWZgw
#3: Protein | Mass: 68009.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||||||||||||||||||
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#7: Protein | Mass: 39706.977 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||||||||||||||||||
#8: Protein | Mass: 101225.328 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||||||||||||||||||||
#9: Protein | Mass: 22062.066 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #12: Protein | | Mass: 101144.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #13: Protein | | Mass: 76154.328 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #14: Protein | Mass: 114163.266 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #16: Protein | | Mass: 94540.883 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #17: Protein | Mass: 23862.807 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #18: Protein | Mass: 22170.178 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #20: Protein | Mass: 50825.766 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #21: Protein | | Mass: 151719.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #22: Protein | | Mass: 124971.133 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #23: Protein | | Mass: 22976.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #24: Protein | | Mass: 152700.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Growth-arrest-specific microtubule-binding ... , 2 types, 2 molecules DE
#4: Protein | Mass: 56190.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#5: Protein | Mass: 55393.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Flagellar associated ... , 2 types, 2 molecules FT
#6: Protein | Mass: 52938.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#19: Protein | Mass: 42931.082 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: CELL / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Combined linker domain of N-DRC and associated proteins Tetrahymena Type: CELL / Entity ID: all / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 45 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 3.6 Å / Resolution method: OTHER / Num. of particles: 211502 / Symmetry type: POINT |