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- EMDB-15977: IFTB1 subcomplex of anterograde intraflagellar transport trains (... -
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Open data
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Basic information
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Title | IFTB1 subcomplex of anterograde intraflagellar transport trains (Chlamydomonas reinhardtii) | |||||||||
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![]() | Cilia / IFT / Intraflagellar / transport / PROTEIN TRANSPORT | |||||||||
Function / homology | ![]() intraciliary transport particle B binding / intraciliary transport involved in cilium assembly / intraciliary transport particle B / outer dynein arm assembly / cilium-dependent cell motility / intraciliary transport / regulation of cilium assembly / : / axoneme assembly / axonemal microtubule ...intraciliary transport particle B binding / intraciliary transport involved in cilium assembly / intraciliary transport particle B / outer dynein arm assembly / cilium-dependent cell motility / intraciliary transport / regulation of cilium assembly / : / axoneme assembly / axonemal microtubule / cilium organization / non-motile cilium assembly / non-motile cilium / motile cilium / ciliary membrane / ciliary base / post-transcriptional regulation of gene expression / beta-tubulin binding / kinesin binding / axoneme / cilium assembly / regulation of microtubule cytoskeleton organization / centriole / tubulin binding / ciliary basal body / regulation of protein stability / cilium / protein transport / apical part of cell / microtubule binding / cytoskeleton / protein stabilization / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | subtomogram averaging / cryo EM / Resolution: 9.9 Å | |||||||||
![]() | Lacey SE / Foster HE / 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
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 28.8 KB 28.8 KB | Display Display | ![]() |
Images | ![]() | 61 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 348.9 KB | Display | ![]() |
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Full document | ![]() | 348.4 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 7.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8bd7MC ![]() 8bdaC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 3.03 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : Two IFTB repeats from anterograde intraflagellar transport trains...
+Supramolecule #1: Two IFTB repeats from anterograde intraflagellar transport trains...
+Macromolecule #1: IFT88
+Macromolecule #2: Osm-6-like protein
+Macromolecule #3: IFT70
+Macromolecule #4: Intraflagellar transport protein 46
+Macromolecule #5: Intraflagellar transport protein 56
+Macromolecule #6: Intraflagellar transport protein 81
+Macromolecule #7: Intraflagellar transport protein 74
+Macromolecule #8: Intraflagellar transport protein 80
+Macromolecule #9: Clusterin-associated protein 1
+Macromolecule #10: Intraflagellar transport protein 57
+Macromolecule #11: Intraflagellar transport particle protein IFT20
+Macromolecule #12: IFT54
+Macromolecule #13: Intraflagellar transport protein 172
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | subtomogram averaging |
Aggregation state | helical array |
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Sample preparation
Buffer | pH: 7 / Details: TAP (Tris-Acetate-Phosphate) Media |
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Grid | Model: Quantifoil R3.5/1 / Material: GOLD |
Vitrification | Cryogen name: ETHANE |
Details | Chlamydomonas reinhardtii cells applied to quantifoil grids and plunge frozen; cilia project out from cell bodies and traverse holes in the carbon film. |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 2.6 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 5.0 µm / Nominal defocus min: 2.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 9.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software: (Name: RELION (ver. 3.1.3), Warp) / Number subtomograms used: 18216 |
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Extraction | Number tomograms: 600 / Number images used: 18216 |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
-Atomic model buiding 1
Refinement | Protocol: FLEXIBLE FIT |
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Output model | ![]() PDB-8bd7: |