Fig. 9: Structural diversity of TEX12 assemblies.
From: Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip
TEX12 adopts a compact dimer structure that undergoes conformational change into an extended tetramer upon FFV mutation. These structures share a common fold in which TEX12 chains interact in a four-helical bundle, stabilised by coiled-coil interactions between their Ctip sites. TEX12 chains adopt a helix–loop–helix conformation within the dimer, and open into linear helices within the tetramer. TEX12 also interacts with SYCE2 to form a 4:4 complex that assembles into fibres within the SC. Within this complex, TEX12 chains adopt linear conformations and orient Ctip sites to mediate assembly by forming four-helical structures with SYCE2’s C-termini. The TEX12 compact dimer, TEX12 tetramer and SYCE2-TEX12 4:4 complex models are shown along with their schematics; TEX12 chains are coloured blue to red in an N- to C-terminal direction and SYCE2 chains are shown in yellow.
