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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | folded state of Tetrahymena IFT-A | |||||||||
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Sample |
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Keywords | intraflagellar transport complex / PROTEIN TRANSPORT | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 8.8 Å | |||||||||
Authors | Ma Y / Wu J / Lei M | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Nat Commun / Year: 2023Title: Structural insight into the intraflagellar transport complex IFT-A and its assembly in the anterograde IFT train. Authors: Yuanyuan Ma / Jun He / Shaobai Li / Deqiang Yao / Chenhui Huang / Jian Wu / Ming Lei / ![]() Abstract: Intraflagellar transport (IFT) trains, the polymers composed of two multi-subunit complexes, IFT-A and IFT-B, carry out bidirectional intracellular transport in cilia, vital for cilia biogenesis and ...Intraflagellar transport (IFT) trains, the polymers composed of two multi-subunit complexes, IFT-A and IFT-B, carry out bidirectional intracellular transport in cilia, vital for cilia biogenesis and signaling. IFT-A plays crucial roles in the ciliary import of membrane proteins and the retrograde cargo trafficking. However, the molecular architecture of IFT-A and the assembly mechanism of the IFT-A into the IFT trains in vivo remains elusive. Here, we report the cryo-electron microscopic structures of the IFT-A complex from protozoa Tetrahymena thermophila. We find that IFT-A complexes present two distinct, elongated and folded states. Remarkably, comparison with the in situ cryo-electron tomography structure of the anterograde IFT train unveils a series of adjustments of the flexible arms in apo IFT-A when incorporated into the anterograde train. Our results provide an atomic-resolution model for the IFT-A complex and valuable insights into the assembly mechanism of anterograde IFT trains. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_34894.map.gz | 195.5 MB | EMDB map data format | |
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| Header (meta data) | emd-34894-v30.xml emd-34894.xml | 11.6 KB 11.6 KB | Display Display | EMDB header |
| Images | emd_34894.png | 43.4 KB | ||
| Others | emd_34894_half_map_1.map.gz emd_34894_half_map_2.map.gz | 170.8 MB 170.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-34894 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-34894 | HTTPS FTP |
-Validation report
| Summary document | emd_34894_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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| Full document | emd_34894_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | emd_34894_validation.xml.gz | 15.3 KB | Display | |
| Data in CIF | emd_34894_validation.cif.gz | 18.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-34894 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-34894 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_34894.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_34894_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_34894_half_map_2.map | ||||||||||||
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Sample components
-Entire : IFT-A_folded
| Entire | Name: IFT-A_folded |
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| Components |
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-Supramolecule #1: IFT-A_folded
| Supramolecule | Name: IFT-A_folded / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: INSILICO MODEL |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 8.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 14020 |
| Initial angle assignment | Type: COMMON LINE |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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About Yorodumi




Keywords
Authors
China, 1 items
Citation









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FIELD EMISSION GUN
