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Figure 5.
Figure 5 Relative movement of the phosphate molecule during the
catalytic cycle. The predicted path of the phosphate molecule
during catalysis is marked by the position of phosphate (or
sulfate) in the  [E]-subunits
of the yF[1]II complex (blue), the bovine AlF[4]^-:ADP-inhibited
structure (Menz et al, 2001) (yellow), and the  -phosphate
of AMPPNP bound to the [DP]-subunit
of the yF[1]I complex (salmon). The structures were superimposed
using the P-loop and neighboring catalytic residues ( 151–177,
330–336).
The  -carbon
trace of the P-loop of all three enzymes is shown along with the
bound nucleotide and phosphate (or sulfate) of yF[1]II (yellow).
The inset shows just the movement of the phosphate relative to
the nucleotide. The phosphate bound to [E]
(blue) moves to the position in the AlF[4]^-:ADP-inhibited state
(yellow) and ends as the -phosphate
of ATP in the DP site (as colored). Also shown is the movement
of Arg375
in the same path. The distances between the atoms are shown in
Å.
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