|
Figure 1.
FIGURE 1. Closed and half-open states of LiPDF. A, the
closed state within the active pH range represented by the
structure determined at pH 7.5. B, the half-open state bound
with actinonin. Shown on the right halves of both A and B, dimer
is formed through hydrophobic interactions (Phe^164, Phe^166,
Met^108, and Met^9 shown in stick model) between two subunits
colored in blue and brown, respectively. Shown on the left
halves of A and B are close-up pictures for the closed and
half-open pockets, respectively (viewed from same direction).
The CD-loop (residue 65-76) is highlighted in red, and the
active zinc ion is in pink. In the closed state (A), the
substrate pocket is blocked and hydrogen bonds are shown by a
green dashed line. For clarity, the formate group is shown as a
star. In the half-open state (B), the bound competitive
inhibitor actinonin is shown in stick-and-dots model. In this
state, Arg^71 is completely solvent-exposed and thus disordered.
This figure and Fig. 3 were prepared using Pymol.
|
