Fig. 3: Crystal structure of a TEX12 ΔCtip tetramer.
From: Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip
a Crystal structure of TEX12 ΔCtip in a tetrameric conformation. The four TEX12 chains (coloured blue to red in an N- to C-terminal direction) are arranged in an anti-parallel configuration with a central ‘hinge’ flanked by two lateral four-helical bundles. b Schematic of the TEX12 ΔCtip structure highlighting the location of missing Ctip sequences in pairs on either side of the 95 Å core. c The hinge is defined by salt-bridges between R78 and D82 amino-acids, and is supported by surrounding aromatic packing interactions of symmetry-related chains (dimer interface), and limited hydrophobic interactions between alternative chains A and B (tetramer interface). d The lateral four-helical bundles contain ‘coiled-coil’-like interactions between symmetry-related chains (dimer interface), and hydrophobic and aromatic interactions between opposing dimers (tetramer interface).
