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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.
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