Fig. 5: The CTD pore-forming domain of Cry78Aa resembles those of aerolysin family toxins. | Communications Biology

Fig. 5: The CTD pore-forming domain of Cry78Aa resembles those of aerolysin family toxins.

From: The crystal structure of Cry78Aa from Bacillus thuringiensis provides insights into its insecticidal activity

Fig. 5

Topology of the aerolysin family of β-pore-forming toxins selected from Dali search results using Cry78Aa155-359 as a model (see Supplementary Table 3). These proteins share a core topology composed of five antiparallel β-sheets and a putative membrane-spanning region (MSR, in yellow). PDB codes are included in parentheses. Any accessory domains outside the pore-forming module (PFM) of the toxins were excluded for clarity. The PFM was divided into two subdomains: a β-sheet subdomain at one side (above the horizontal gray line) and a β-sandwich subdomain at the opposite side (below the horizontal gray line). The secondary structure, including length, twist, number of β-sheets, and putative membrane-spanning region (in yellow), varies widely among the selected toxins. However, in all cases the putative MSR region is located between the second and third sheets, suggesting that these toxins might share a common mechanism of pore formation.

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