Figure 8.

Homology model of the C-linker and CNBD domains of KAT2. A, Assembly of the KAT2 C-linker and CNBD domains in a tetrameric configuration. One subunit is shown in ribbon display, while the other three are depicted in globular display, with each subunit colored differently. B, Ribbon representation of the KAT2 region (Met-295 to Gly-499) encompassing the end of the last transmembrane segment (S6), the C-linker domain (six α-helices [A′ to F′] separated by short loops), and the CNBD (one α-helix [A], a β-roll formed by β-strands, followed by two α-helices [B and C]). The α-helices are shown in red, and the β-strands are shown in green-yellow. The positions of the three sequences identified in this article (₃₁₂TVRAASEFA₃₂₀, ₃₈₁VS₃₈₂, and ₃₉₂DIDAE₃₉₆) are highlighted in orange, blue, and purple, respectively, and their corresponding side chains are displayed. C and D, Closeups of A′ and B′ α-helices of the KAT2 C-linker containing the native ₃₁₂TVRAASEFA₃₂₀ (C) and the mutated ₃₁₂AINDILRYT₃₂₀ (D) sequences. E and F, Closeups of the linker residues between F′ and A α-helices containing the native ₃₈₁VS₃₈₂ (E) and the mutated V381F/S382P (F) sequences.