8F5P

Structure of Leishmania tarentolae IFT-A (state 2)

Summary for 8F5P

• Entry DOI: 10.2210/pdb8f5p/pdb
• EMDB information: 28867
• Descriptor: NET domain-containing protein, Intraflagellar transport protein 122B, putative, Intraflagellar transport protein 122 homolog, ... (7 entities in total)
• Functional Keywords: cilia, ift, protein transport
• Biological source: Leishmania tarentolae; More
• Total number of polymer chains: 6
• Total formula weight: 839002.27

Authors

Zhou, H.,Brown, A. (deposition date: 2022-11-14, release date: 2022-12-21, Last modification date: 2024-05-22)

Primary citation

Meleppattu, S.,Zhou, H.,Dai, J.,Gui, M.,Brown, A.
Mechanism of IFT-A polymerization into trains for ciliary transport.
Cell, 185:4986-, 2022

PubMed Abstract: Intraflagellar transport (IFT) is the highly conserved process by which proteins are transported along ciliary microtubules by a train-like polymeric assembly of IFT-A and IFT-B complexes. IFT-A is sandwiched between IFT-B and the ciliary membrane, consistent with its putative role in transporting transmembrane and membrane-associated cargoes. Here, we have used single-particle analysis electron cryomicroscopy (cryo-EM) to determine structures of native IFT-A complexes. We show that subcomplex rearrangements enable IFT-A to polymerize laterally on anterograde IFT trains, revealing a cooperative assembly mechanism. Surprisingly, we discover that binding of IFT-A to IFT-B shields the preferred lipid-binding interface from the ciliary membrane but orients an interconnected network of β-propeller domains with the capacity to accommodate diverse cargoes toward the ciliary membrane. This work provides a mechanistic basis for understanding IFT-train assembly and cargo interactions.

PubMed: 36563665
DOI: 10.1016/j.cell.2022.11.033

Experimental method

ELECTRON MICROSCOPY (3.4 Å)