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Figure 2.
FIGURE 2. A, structure of R7 GAT bound to acetyl coenzyme A
(ACO, magenta) and the competitive inhibitor, 3PG (green). B,
molecular surface of the R7 GAT ternary complex colored by its
electrostatic potential reveals the electropositive
substrate-binding site. Acetyl coenzyme A and 3PG are shown in
the active site cleft. C, close up of the active site. Polar
contacts made by 3PG are indicated (gray dashes), and water
molecules are shown as red spheres. Modeling glyphosate into the
active site positions its 2° amine (equivalent position on
3PG marked with an asterisk) within 3.8 Å of the carbonyl
carbon of AcCoA. D, shuffling changes are distributed throughout
the enzyme. A C-  trace indicates the
locations of 21 amino acid substitutions (yellow and blue
spheres) made between native and R7 GAT. Substitutions located
within 5 Å of either ligand are shown in blue.
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