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Figure 5
Variation of intermediate binding modes of the hSQS mutants. (a) The final 2Fo − Fc electron-density maps for PSPP (cyan) and residue Ala288 at 2.0 Å resolution are contoured at 1.0σ (grey) and 2.0σ (pink). (b) Comparison of binding modes of PSPP between the F288A mutant and wild-type hSQS (green and yellow). (c) PSPP binding in the active site of the F288L mutant. The final 2Fo − Fc electron-density maps for PSPP (grey) and residue Leu288 at 1.85 Å resolution are contoured at 1.0σ (grey) and 2.0σ (pink). (d) Superimposition of the F288L mutant and wild-type hSQS (green with yellow) illustrates the similar binding conformation of PSPP. |