Figure 3.
FIG. 3. ttLC-FACS crystal structure. Ribbon representations
of the ttLC-FACS dimer are shown (A). In the panel, the
secondary structure of the C-terminal domain is colored in
green. In the N-terminal domain, -helix and -sheet
are colored in cyan and red, respectively, with the N-terminal
domain-swapping peptide colored in yellow. The electrostatic
potential surface map of ttLC-FACS dimer in the same orientation
as the representation in A. Red represents negatively charged
regions, and blue represents positively charged regions (B).
Close-up view of the N-terminal peptide involved in domain
swapping in the reverse orientation view to A (C). Residues with
carbons colored in pink against a cyan surface of one monomer
interacts with the concave surface of the other monomer colored
in yellow. There are salt bridges at the domain swapping region.
The monomer of ttLC-FACS with each secondary structure feature
is labeled according to the scheme given in Fig. 2A (D).
-helix and 
-sheet
are colored in cyan and red, respectively, with the N-terminal
domain-swapping peptide colored in yellow. The electrostatic
potential surface map of ttLC-FACS dimer in the same orientation
as the representation in A. Red represents negatively charged
regions, and blue represents positively charged regions (B).
Close-up view of the N-terminal peptide involved in domain
swapping in the reverse orientation view to A (C). Residues with
carbons colored in pink against a cyan surface of one monomer
interacts with the concave surface of the other monomer colored
in yellow. There are salt bridges at the domain swapping region.
The monomer of ttLC-FACS with each secondary structure feature
is labeled according to the scheme given in Fig. 2A (D).