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Figure 2.
Fig. 2. Structure of FliI(  1–18). (A) C^  ribbon
drawing of FliI( 1–18). 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. (C–F) Comparison of the relative domain
orientation. FliI( 1–18) (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).
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