 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](gx5204fig2mag.jpg)
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Figure 2
(a) Measurement of the binding of 3-MeA to S. aureus TAG using intrinsic fluorescence quenching at pH 5.8 (Kd = 165 µM) and pH 7.8 (Kd = 78 µM); the results are similar to those previously reported for the E. coli enzyme (Cao et al., 2003  ). (b) Fluorescence quenching of 3-MeA with E38Q-mutant S. aureus TAG at pH 5.8 and 7.8. The small reduction in the binding constant was inconsistent with structural and previous functional data (Cao et al., 2003). This indicated that the fluorescence was unreliable for the S. aureus enzyme. (c) ITC measurement of the binding of 3-MeA to S. aureus TAG at pH 7.8 (Kd = 220 µM) and pH 5.8 (Kd = 470 µM). Adenosine does not bind. (d) ITC measurement of the binding of 3-MeA to Y16F-mutant (Kd = 1.2 mM; left) and E38Q-mutant (no binding; right) S. aureus TAG at pH 7.8. 1 cal = 4.186 kJ. |
![[Figure 2]](gx5204fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
