Figure 2.
Fig. 2. Structure of the Rdx–RdxR complex. (A) Cartoon
representation. RdxR colors are as in Fig. 1A, and Rdx is in
dark red. FAD, modeled NADH (translucent), and cysteine residues
of the iron-binding site are shown in ball-and-stick mode, and
Fe^3+ is shown as a green sphere. Anomalous-difference electron
density (red) contoured at 6.0 documents the presence
of the Fe^3+. Amino acid exchanges between RubA1 and RubA2 are
indicated as spheres in Rdx (conservative, orange;
nonconservative, blue). (B) Interactions surrounding the
redox-active site of the complex. Interacting residues are shown
as ball-and-stick models (C of RdxR, yellow, and of Rdx,
red-brown). FAD is shown in ball-and-stick mode. (C) Binding
curves for the interaction of RdxR to Fe^3+ (red)- and Ni^2+
(green)-substituted Rdx.
documents the presence
of the Fe^3+. Amino acid exchanges between RubA1 and RubA2 are
indicated as spheres in Rdx (conservative, orange;
nonconservative, blue). (B) Interactions surrounding the
redox-active site of the complex. Interacting residues are shown
as ball-and-stick models (C of RdxR, yellow, and of Rdx,
red-brown). FAD is shown in ball-and-stick mode. (C) Binding
curves for the interaction of RdxR to Fe^3+ (red)- and Ni^2+
(green)-substituted Rdx.