8BD7
IFTB1 subcomplex of anterograde Intraflagellar transport trains (Chlamydomonas reinhardtii)
This is a non-PDB format compatible entry.
Summary for 8BD7
| Entry DOI | 10.2210/pdb8bd7/pdb |
| EMDB information | 15977 15978 15979 16014 |
| Descriptor | IFT88, Intraflagellar transport protein 57, Intraflagellar transport particle protein IFT20, ... (13 entities in total) |
| Functional Keywords | cilia, ift, intraflagellar, transport, protein transport |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 26 |
| Total formula weight | 1832357.52 |
| Authors | Lacey, S.E.,Foster, H.E.,Pigino, G. (deposition date: 2022-10-18, release date: 2023-01-11, Last modification date: 2024-11-13) |
| Primary citation | Lacey, S.E.,Foster, H.E.,Pigino, G. The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains. Nat.Struct.Mol.Biol., 30:584-593, 2023 Cited by PubMed 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 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. PubMed: 36593313DOI: 10.1038/s41594-022-00905-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9.9 Å) |
Structure validation
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