|
Figure 3.
Enzyme interactions with the Ala quinonoid intermediate in
the closed (A) and open (B) active sites. Stereo views with
structures of quinonoid and two water molecules superposed with
the corresponding weighted |F[o]| - |F[c]| electron density omit
maps (green) are contoured at the 3.0σ level. Hydrogen bonds
are denoted by dashed lines. Carbon atoms of residues belonging
to the large rigid region are shown in orange, those from the
small rigid region are shown in pink, and the residues from the
neighboring subunit are shown in blue and labeled with a star.
The alternate conformations of Thr-124, Thr-216, Met-288, and
Phe-449 in the open conformation are shown in corresponding pale
tones.
|
