Extended Data Fig. 5: Structural modelling of the interaction between PEX7 and the KPWE motif of PEX13.

a, Interaction between full-length yeast PEX7 and residues 1–27 (including the KPWE motif) of yeast PEX13, predicted by AlphaFold. PEX7 is shown as a space-filling model in the same orientation as in Fig. 3c, coloured by surface electrostatic potential according to the scale on the right. The PEX13 fragment is depicted as a ribbon, with the side chain of lysine 10 (K10) of the KPWE motif shown. The region outlined by a dashed black line is magnified on the right. b, As above, with PEX7 coloured by surface hydrophobicity according to the scale on the right, and showing the side chain of proline 11 (P11) of the KPWE motif. c, As above, with PEX7 coloured yellow and showing the side chain of glutamate 13 (E13) of the KPWE motif. E13 is predicted to contact arginine 117 (R117) within the loop of one of the WD40 blades of the PEX7 β-propeller (overlaid on top as a cartoon representation). A sequence alignment of this loop from the indicated organisms is shown on the right, illustrating the conservation of the arginine residue. d, As in panel c, with the model rotated as indicated and showing the side chain of tryptophan 12 (W12) of the KPWE motif. W12 is predicted to contact the aliphatic stem of lysine 230 (K230) within the loop of one of the WD40 blades of the PEX7 β-propeller (overlaid on top as a cartoon representation). A sequence alignment of this loop from the indicated organisms is shown on the right, illustrating the conservation of the lysine residue.