Figure 3.
Fig. 3. The active site of CT and the binding mode of CoA. (A)
Schematic drawing in stereo of the active site of CT. The N
domain is shown in cyan, and the C domain of the other monomer
is shown in green. The side chains of residues in the active
site are shown in purple. The prime (') in the labels indicates
the C domain of the other monomer of the dimer. (B) Molecular
surface of the active site region of CT. The side chain of
Lys1764 (in helix 6, 15
Å from the active site) has been removed to facilitate the
viewing of the active site. (C) Chemical structure of haloxyfop
and the double reciprocal plot showing the competitive
inhibition of wild-type yeast CT by haloxyfop. (A) was produced
with Ribbons (22), and (B) with Grasp (23).
The above figure is reprinted
by permission from the AAAs:
Science
(2003,
299,
2064-2067)
copyright 2003.
6, 15
Å from the active site) has been removed to facilitate the
viewing of the active site. (C) Chemical structure of haloxyfop
and the double reciprocal plot showing the competitive
inhibition of wild-type yeast CT by haloxyfop. (A) was produced
with Ribbons (22), and (B) with Grasp (23).