Fig. 1: Structure of Hsp90-Cdc37-PINK1 reveals the mechanism of PINK1 loading.
From: Molecular mechanism of PINK1 regulation by the Hsp90 machinery
a Composite cryo-EM map of the Hsp90-Cdc37-PINK1 complex in front and back views. b Atomic model of the Hsp90-Cdc37-PINK1 complex represented as a cartoon, with boxes corresponding to the details shown in panels (d–h). c Comparison of the PINK1 structure in the Hsp90-Cdc37-PINK1 complex and the Pediculus humanus corporis PINK1 (PDB: 6EQI), with PhPINK1 colored in pink and PINK1 in the Hsp90- Cdc37-PINK1 complex colored in yellow. Ins3 and β5 of phPINK1 is colored in red. d Interface between the Hsp90 lumen and the PINK1 polypeptide, with Hsp90A and Hsp90B depicted by the density map and PINK1 shown using a transparent map alongside a cartoon and stick model. e Interface of the Hsp90 lumen and the PINK1 polypeptide, with Hsp90 lumen shown in surface representation colored by hydrophobicity, and five hydrophobic residues of PINK1 depicted in stick format. f Interface between Hsp90B and the PINK1 polypeptide and αD helix. g Detailed view of the interaction between the Cdc37 N-terminal domain and the Hsp90 dimer, with Hsp90 dimer shown in surface representation, and the coiled-coil domain of Cdc37 hidden for clarity. The phosphorylated S13 is labeled as pS13. h Details of the interface between the Cdc37 N-terminal hook loop and the PINK1 C-lobe. Hsp90A is colored cyan, Hsp90B marine, PINK1 yellow, and Cdc37 salmon. The CTE domain of PINK1 is highlighted in green.
