Fig. 2: Vip3Bc1act has a greater propensity to perturb liposome membranes compared with Vip3Bc1. | Nature Communications

Fig. 2: Vip3Bc1act has a greater propensity to perturb liposome membranes compared with Vip3Bc1.

From: Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane

Fig. 2

A Digestion of the complex increases activity according to CF dye release from LUVs upon addition of Vip3Bc1act (red) and Vip3Bc1 (grey). Plotted data represents the mean and the error bars the standard deviation of the measurements from three independent replicates (Full data shown Supplementary Table 3 and 4). B Quaternary structure of Vip3Bc1act tetramer as shown from two views of the complex related by 90° for the EM density (I, ii) and model (iii, iv). C Model of Vip3Bc1act asymmetric unit, illustrating domain structure as a monomer. D Vip3Bc1act tetrameric assembly as shown from the top conformation is consistent with a pore. E Pore structure of Vip3Bc1act.

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