Extended Data Fig. 6: Location of disease-causing point mutations and of phospholipid and cholesterol molecules.

a, A side view of the model for the ligase complex, with helices as cylinders. Point mutations found in patients in PEX2, PEX10, or PEX12 are indicated as balls in different colors. The specific mutations and the corresponding positions in the T. thermophilus (T.t.) proteins are listed on the side. b, A magnified view of the RFs from the cytosol, with disease mutations highlighted. The long isoform of Pex10 (UniProtKB – O60683-2) was used for residue numbering. c, Space-filling model of the ligase complex in two different side views. Amino acids are colored according to the degree of their hydrophobicity (scale below the arrow). Cryo-EM density modeled as phospholipid or ergosterol molecules is colored in purple. d, Examples of phospholipid and ergosterol molecules plugging holes in the channel walls. Shown is a cut through the semi-transparent space-filling and embedded cartoon models. For phospholipids, the modeled head groups and acyl chains are indicated.