|
Figure 3.
Fig. 3. RIIβ holoenzyme assumes a closed confirmation: (a)
shows three holoenzyme structures with the trapped transition
state that is present in the RIIβ holoenzyme structure
(middle). The RIIα holoenzyme (left) is in an open form whereas
the RIIβ and RIα complexes (right) are in a closed
conformation. The color designations are as follows: E230^C,
E170^C, and E203^C are shown in red and provide the acidic
docking surface for the P − 3 and P − 2 arginines; the P + 1
pocket (L198^C and P202^C) is in white and provides the
hydrophobic site for the P + 1 residue; Y330^C in the C-tail is
yellow; the glycine rich loop is in pink; AMP-PNP is in black.
The temperature factors analysis of the C subunit in three
holoenzyme structures is shown in (b). Shown on the left is
RIIα(90–400):C in the absence of ATP (2QVS), with the
disordered/mobile regions underlined in red; in the middle is
RIIβ(108–268):C:AMP-PNP; on the right is
RIα(91–244):C:AMP-PNP (1U7E).
|
