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Figure 4.
Fig. 4. Close-up views of the active site and the two
clusters of the mutated residues. The residues are colored as
shown in Fig. 2. The structure of the ATB17-isovalerate complex
is indicated by thick gray lines and that of the wild-type
AspAT-maleate complex is indicated by thin purple lines. A,
several water molecules are introduced into the active site of
ATB17 (light blue spheres). One water molecule (WAT1) is located
at almost the same position as a water molecule observed in the
wild-type AspAT (a purple sphere). Arg292, Val293, and Ser297
belong to the other subunit of the dimer (asterisks). B and C,
viewed from the same direction as in Fig. 2.
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