Skip to main content
Fig. 1 | BMC Biology

Fig. 1

From: The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins

Fig. 1

Crystal structure of Cry6a toxin. Ribbon representation of trypsin-truncated Cry6Aa form showing two domain architecture: the “tail” domain consists of one helical bundle with five long α-helices, labeled αA, αC, αD, αG, and αH, and shorter helices, labeled αB, αE, αF, and αI; while several long and short loops form the “head” domain. N- and C-termini and the putative transmembrane region are labeled. The Cys88-Cys451 disulfide bond is shown and, in the insert box, the final 2Fo-Fc electron density map calculated at 1.5σ in the region of this bond is shown in blue mesh. Side and main chains of the amino acid residues are presented as sticks and colored by the atoms

Back to article page