6IAE

T. brucei IFT22 GDP-bound crystal structure

Summary for 6IAE

• Entry DOI: 10.2210/pdb6iae/pdb
• Related: 6IA7
• Descriptor: Intraflagellar transport protein 22, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: intraflagellar transport protein 22, cilium formation, rab-like, gtpase, rabl5, cytosolic protein
• Biological source: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
• Total number of polymer chains: 2
• Total formula weight: 50664.54

Authors

Wachter, S.,Basquin, J.,Lorentzen, E. (deposition date: 2018-11-26, release date: 2019-04-10, Last modification date: 2024-05-15)

Primary citation

Wachter, S.,Jung, J.,Shafiq, S.,Basquin, J.,Fort, C.,Bastin, P.,Lorentzen, E.
Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly.
Embo J., 38:-, 2019

PubMed Abstract: Intraflagellar transport (IFT) relies on motor proteins and the IFT complex to construct cilia and flagella. The IFT complex subunit IFT22/RabL5 has sequence similarity with small GTPases although the nucleotide specificity is unclear because of non-conserved G4/G5 motifs. We show that IFT22 specifically associates with G-nucleotides and present crystal structures of IFT22 in complex with GDP, GTP, and with IFT74/81. Our structural analysis unravels an unusual GTP/GDP-binding mode of IFT22 bypassing the classical G4 motif. The GTPase switch regions of IFT22 become ordered upon complex formation with IFT74/81 and mediate most of the IFT22-74/81 interactions. Structure-based mutagenesis reveals that association of IFT22 with the IFT complex is essential for flagellum construction in although IFT22 GTP-loading is not strictly required.

PubMed: 30940671
DOI: 10.15252/embj.2018101251

Experimental method

X-RAY DIFFRACTION (2.49 Å)