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Figure 3.
Fig. 3. The Mg2+-catalyzed phosphoryl transferase activity. (A)
Overview of Mg: AMPPCP binding, shown with a ball-and-stick
representation of interacting residues. The color scheme is the
same as in Fig. 1C. The bent conformation of the nucleotide,
stabilized primarily by three arginines, can be seen. (B)
Coordination of the  -phosphate and
Asp351 by a magnesium ion. The Asp351 side chain is still far
from the -phosphorus atom.
(C) The transition state of phosphoryl transfer as mimicked by
ADP:AlF[4]^-. The Mg2+ ion coordinates Asp351 and AlF[4]^-, and
the ß-phosphate and the Asp351 side chain form tight
coordination of the aluminum atom as indicated by dashed lines
in color. Residues important for stabilization are indicated.
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