Figure 1 - full size

 

Figure 1.
FIGURE 1. A, sequence alignment of the C-terminal domain of PezA and PezT with the epsilon/zeta system. Identical residues are colored green, highly homologous residues orange, and homologous residues yellow, respectively. Secondary structures are shown above the sequence alignment with -helices illustrated as cylinders and -strands as arrows. The region in PezT that could not be modeled into the electron density is indicated by a green line. Residues that are involved in PezA-PezA interaction are labeled with filled squares beneath the sequence alignment, and those that are involved in PezA-PezT interaction with filled triangles. Open circles label residues of PezA that inhibit the toxin PezT. Asterisks indicate those residues that were changed by site-directed mutagenesis in PezT and were shown to abolish PezT toxicity. Filled diamonds above the sequence alignment indicate residues of different PezT variants where mutations to homologous residues were observed, open diamonds mark mutations of a non-conservative nature. B, ribbon representation of the heterotetrameric PezA/PezT arrangement. Helices of PezA are colored in blue and helices of PezT in beige, respectively. -Strands in PezT are colored in red. C, surface representation of the complex colored according to the color scheme of A.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 19606-19618) copyright 2007.