Extended Data Fig. 8: Interactions between Erf2 and Erf4.
From: Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation
a, The overall structure of the Erf2-Erf4 complex. b, Residues R126, R216 and S329 in TM2, TM3 and the PPII helix of Erf2 interact with residues G176, S179, N164 and R222 in α4′-α8′ helices of Erf4 through hydrogen bonding. P325 and P328 in the PPII helix of Erf2 dock into to hydrophobic pockets in Erf4. c, Residues T162, H163, S165 and I166 in Erf2 form hydrogen bonds with residues R17 and R83 in Erf4. d, e, The linker between the TM2 and β1 strand of Erf2 interacts with the N-terminal region and the loop between β2′ and β3′ of Erf4 through hydrogen bonding, π–π stacking and CH-π interactions. The hydrogen bonds are represented by yellow dashed lines.
