Figure 2 - full size


Figure 2.
Fig. 2. Structure of FliI( 1ā€“18). (A) C^ ribbon drawing of FliI( 1ā€“18). All of the secondary structure elements are labeled as in Fig. 1. The linker connecting the N-terminal and ATPase domains, which is missing in the model, is indicated by a dashed line. (B) Close-up stereoview of the nucleotide-binding site. The bound ADP is colored green, and the residues interacting with ADP are shown in cyan. Conserved residues involved in catalysis are indicated by yellow. (Cā€“F) Comparison of the relative domain orientation. FliI( 1ā€“18) (cyan) is superimposed onto the F[1]- subunits in various states, for which only corresponding atoms in the ATPase domain were used for fitting: (C) [E] (green), (D) [TP] (magenta), (E) [DP] (yellow) in 1BMF (21), and (F) [ADP+Pi] (red) in 1H8E (22).