8HME

head module state 1 of Tetrahymena IFT-A

Summary for 8HME

• Entry DOI: 10.2210/pdb8hme/pdb
• EMDB information: 34896 34897
• Descriptor: Intraflagellar transport protein 122 homolog, Intraflagellar transporter, WD40 repeat protein, ... (4 entities in total)
• Functional Keywords: intraflagellar transport complex, protein transport
• Biological source: Tetrahymena thermophila; More
• Total number of polymer chains: 3
• Total formula weight: 464127.07

Authors

Ma, Y.,Wu, J.,Lei, M. (deposition date: 2022-12-03, release date: 2023-06-14, Last modification date: 2024-07-03)

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

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: 36932088
DOI: 10.1038/s41467-023-37208-2

Experimental method

ELECTRON MICROSCOPY (4.2 Å)