Fig. 1: Protoxin structure of Vip3Aa from Bacillus thuringiensis.
From: Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis
a Two orthogonal views of the Vip3Aa protoxin. Each monomer has been colored differently. Yellow stars mark the position of the trypsin cleavage site in two of the monomers. Unsharpened EM map shown on the left. b Primary structure of Vip3Aa. c Vip3Aa is formed by two types of monomers, outer (left), and inner (right), that are mainly differentiated by a ~90° rotation of the α2–α3 helical bundle. d Vip3Aa tetramer colored according to the domain organization. Two orthogonal views of the EM reconstruction are shown on the right.
