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. 2018 Apr 16;7:e33067. doi: 10.7554/eLife.33067

Figure 2. Crystal structure of the IFT80 protein.

(A) Structural overview showing the overall domain organization of CrIFT80. It contains two N-terminal β-propellers (coloured in red and orange) connected by a long strand and interacting with each other via several loops. A helical extension in β-propeller two keeps the C-terminal α-solenoid region (coloured in yellow) in position. (B) β-propeller one displays a canonical fold of a 7-bladed WD40 β-propeller. The most N-terminal β-strand forms the outermost strand of blade 7, effectively closing the ring-shaped structure by linking blade 7 to blade 1. Individual β-strands are numbered and the blade numbers are indicated in white circles. (C) β-propeller two displays an unusual open conformation where the incomplete blade seven lacks the outermost β-strand. Individual β-strands are numbered and the blade numbers are indicated in white circles. (D) Superpositioning of the CrIFT80 structure (coloured as in (A)) with the evolutionarily related β’COP protein (pdb: 3MKQ; coloured in grey). The two structures differ significantly with respect to the positions of β-propeller two as well as the α-solenoid C-terminus. (E) Isolated view on β-propeller 2 of β’COP (pdb:3MKQ, coloured in grey). Although this propeller also lacks the outermost strand in blade 7, it is closed by an extended loop in blade 1 (coloured in red).

Figure 2.

Figure 2—figure supplement 1. Sequence alignment between IFT80 proteins from various species.

Figure 2—figure supplement 1.

IFT80 sequences from six organisms were aligned using Clustal Omega (McWilliam et al., 2013), and the resulting aligment was visualized in ESPript (Robert and Gouet, 2014). Secondary structure elements derived form the structure of CrIFT80 presented in this work are shown in black above the alignment. Predicted secondary structure elements for the most C-terminal region for which no electron density was observed in the crystal are shown in grey. Red arrowheads below the alignment show the positions of mutated residues in ciliopathy patients with alterations in IFT80.