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- PDB-8bd7: IFTB1 subcomplex of anterograde Intraflagellar transport trains (... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8bd7 | |||||||||
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Title | IFTB1 subcomplex of anterograde Intraflagellar transport trains (Chlamydomonas reinhardtii) | |||||||||
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![]() | PROTEIN TRANSPORT / Cilia / IFT / Intraflagellar / transport | |||||||||
Function / homology | ![]() intraciliary transport particle B binding / intraciliary transport particle / intraciliary transport involved in cilium assembly / intraciliary transport particle B / cilium-dependent cell motility / outer dynein arm assembly / intraciliary transport / regulation of cilium assembly / axoneme assembly / axonemal microtubule ...intraciliary transport particle B binding / intraciliary transport particle / intraciliary transport involved in cilium assembly / intraciliary transport particle B / cilium-dependent cell motility / outer dynein arm assembly / intraciliary transport / regulation of cilium assembly / axoneme assembly / axonemal microtubule / cilium organization / protein localization to cilium / non-motile cilium assembly / non-motile cilium / motile cilium / ciliary membrane / post-transcriptional regulation of gene expression / ciliary base / beta-tubulin binding / microtubule organizing center / kinesin binding / axoneme / cilium assembly / regulation of microtubule cytoskeleton organization / centriole / tubulin binding / ciliary basal body / regulation of protein stability / cilium / apical part of cell / protein transport / microtubule binding / cytoskeleton / protein stabilization / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 9.9 Å | |||||||||
![]() | Lacey, S.E. / Foster, H.E. / Pigino, G. | |||||||||
Funding support | European Union, ![]()
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![]() | ![]() Title: The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains. Authors: Samuel E Lacey / Helen E Foster / Gaia Pigino / ![]() Abstract: Anterograde intraflagellar transport (IFT) trains are essential for cilia assembly and maintenance. These trains are formed of 22 IFT-A and IFT-B proteins that link structural and signaling cargos to ...Anterograde intraflagellar transport (IFT) trains are essential for cilia assembly and maintenance. These trains are formed of 22 IFT-A and IFT-B proteins that link structural and signaling cargos to microtubule motors for import into cilia. It remains unknown how the IFT-A/-B proteins are arranged into complexes and how these complexes polymerize into functional trains. Here we use in situ cryo-electron tomography of Chlamydomonas reinhardtii cilia and AlphaFold2 protein structure predictions to generate a molecular model of the entire anterograde train. We show how the conformations of both IFT-A and IFT-B are dependent on lateral interactions with neighboring repeats, suggesting that polymerization is required to cooperatively stabilize the complexes. Following three-dimensional classification, we reveal how IFT-B extends two flexible tethers to maintain a connection with IFT-A that can withstand the mechanical stresses present in actively beating cilia. Overall, our findings provide a framework for understanding the fundamental processes that govern cilia assembly. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.9 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 275.6 KB | Display | |
Data in CIF | ![]() | 420.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 15977MC ![]() 8bdaC 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
-Protein , 6 types, 12 molecules AHBJCKLTWYXZ
#1: Protein | Mass: 86418.125 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 50453.184 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: Protein | Mass: 74248.609 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#9: Protein | Mass: 49733.469 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#11: Protein | Mass: 15658.664 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#12: Protein | Mass: 54437.715 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Intraflagellar transport protein ... , 7 types, 14 molecules DNEOFPGQIRMUSV
#4: Protein | Mass: 37976.410 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#5: Protein | Mass: 63485.508 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#6: Protein | Mass: 77186.484 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#7: Protein | Mass: 71648.398 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#8: Protein | Mass: 85782.609 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#10: Protein | Mass: 51298.414 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#13: Protein | Mass: 197851.172 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: HELICAL ARRAY / 3D reconstruction method: subtomogram averaging |
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Sample preparation
Component | Name: Two IFTB repeats from anterograde intraflagellar transport trains within native Chlamydomonas reinhardtii cilia Type: COMPLEX / Entity ID: all / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7 / Details: TAP (Tris-Acetate-Phosphate) Media |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: Chlamydomonas reinhardtii cells applied to quantifoil grids and plunge frozen; cilia project out from cell bodies and traverse holes in the carbon film. |
Specimen support | Grid material: GOLD / Grid type: Quantifoil R3.5/1 |
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: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 5000 nm / Nominal defocus min: 2500 nm |
Specimen holder | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 2.6 e/Å2 / Avg electron dose per subtomogram: 104 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.20.1_4487: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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CTF correction | Details: Warp/Relion/M - CTF Refinement in M / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 9.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 18216 / Symmetry type: POINT | ||||||||||||||||||||||||
EM volume selection | Num. of tomograms: 600 / Num. of volumes extracted: 18216 | ||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT | ||||||||||||||||||||||||
Refine LS restraints |
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