5N4A

Crystal structure of Chlamydomonas IFT80

Summary for 5N4A

• Entry DOI: 10.2210/pdb5n4a/pdb
• Descriptor: Intraflagellar transport protein 80, GLYCEROL, OXALATE ION, ... (4 entities in total)
• Functional Keywords: cilium, intraflagellar transport, ift80, transport protein
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 1
• Total formula weight: 87896.74

Authors

Taschner, M.,Mourao, A. (deposition date: 2017-02-10, release date: 2018-02-28, Last modification date: 2024-05-08)

Primary citation

Taschner, M.,Lorentzen, A.,Mourao, A.,Collins, T.,Freke, G.M.,Moulding, D.,Basquin, J.,Jenkins, D.,Lorentzen, E.
Crystal structure of intraflagellar transport protein 80 reveals a homo-dimer required for ciliogenesis.
Elife, 7:-, 2018

PubMed Abstract: Oligomeric assemblies of intraflagellar transport (IFT) particles build cilia through sequential recruitment and transport of ciliary cargo proteins within cilia. Here we present the 1.8 Å resolution crystal structure of the IFT-B protein IFT80, which reveals the architecture of two N-terminal β-propellers followed by an α-helical extension. The N-terminal β-propeller tethers IFT80 to the IFT-B complex via IFT38 whereas the second β-propeller and the C-terminal α-helical extension result in IFT80 homo-dimerization. Using CRISPR/Cas to create biallelic frameshift mutations in IMCD3 mouse cells, we demonstrate that IFT80 is absolutely required for ciliogenesis. Structural mapping and rescue experiments reveal that human disease-causing missense mutations do not cluster within IFT80 and form functional IFT particles. Unlike missense mutant forms of IFT80, deletion of the C-terminal dimerization domain prevented rescue of ciliogenesis. Taken together our results may provide a first insight into higher order IFT complex formation likely required for IFT train formation.

PubMed: 29658880
DOI: 10.7554/eLife.33067

Experimental method

X-RAY DIFFRACTION (1.79 Å)