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Figure 2.
FIG. 2. The structure of tryparedoxin. a, a ribbon diagram
depicting the TryX fold, secondary structure assignment, and
location of the redox-active disulfide formed between Cys-40 and
Cys-43 (yellow sticks). Figs. 2a and 3, 4,5 were prepared with
MOLSCRIPT (39) and RASTER3D (40). In b, the amino acid sequence
of residues colored red are strictly conserved, and those
colored black are similar at scale 7 in the ALSCRIPT program
(41). The active site motif WCPPCR is marked with o .
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