Summary for 8HMD
| Entry DOI | 10.2210/pdb8hmd/pdb |
| EMDB information | 34895 34896 |
| Descriptor | Intraflagellar transport protein 122 homolog, WD40 repeat protein, Tetratricopeptide repeat protein, ... (5 entities in total) |
| Functional Keywords | intraflagellar transport complex, protein transport |
| Biological source | Tetrahymena thermophila More |
| Total number of polymer chains | 4 |
| Total formula weight | 453074.56 |
| Authors | |
| Primary citation | Ma, Y.,He, J.,Li, S.,Yao, D.,Huang, C.,Wu, J.,Lei, M. Structural insight into the intraflagellar transport complex IFT-A and its assembly in the anterograde IFT train. Nat Commun, 14:1506-1506, 2023 Cited by PubMed 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 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. PubMed: 36932088DOI: 10.1038/s41467-023-37208-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.7 Å) |
Structure validation
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