Fig. 2: Molecular architecture of the α-LTX pore.
From: Structural basis of α-latrotoxin transition to a cation-selective pore
a Representative α-LTX particle on a POPC-liposome in negative stain EM. From 988 micrographs, a total of 108 similar particles were used to create a 2D class average as shown in (b). The individual domains of the toxins are highlighted (CD connector domain, HBD helical bundle domain, PD β-sheet plug domain, ARD ankyrin repeat domain). c AlphaFold2 prediction of a tetrameric assembly of residues E21–E360 of α-LTX. The surface coulombic electrostatics [kcal/(mol·e)] indicates a membrane-spanning domain at its N-terminus. d Molecular model of the complete α-LTX pore obtained by combining the cryo-EM structure and the AlphaFold2 prediction overlaid in the negative stain average of α-LTX pore on liposomes. e Structural rearrangements of the CD lead to the formation of an extended coiled-coil and the TMD.
