FIGURE 1.
Nro1ΔN54 structure. (A) Ribbon representation of the Nro1ΔN54 monomer. Each TPR unit is represented with different colors. Helices A and B are in dark and light colors, respectively. (B) Superposition of the Nro1-C domain (light green) onto the Nro1-N domain (orange). (C) Ribbon representation of the superimposition of the C-P4H TPR domain (beige) onto the Nro1-C domain (same color-code as panel A). The Tyr side-chains from C-P4H TPR domains that have been shown to be involved in substrate binding are depicted as sticks. (D) Mapping of the residue conservation at the surface of Nro1-C domain. Color-coding is from white (no conservation) to cyan (high conservation). To facilitate the comparison, the same scale of sequence conservation has been used in all the figures. The orientation is similar to panel C. For clarity, the C-P4H TPR domain has been omitted.