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Figure 4.
Fig. 4. Comparison of the active sites of Yersinia PTPase and
E. coli alkaline phosphatase (Protein Data Bank entry 1ALK).
Alkaline phosphatase is indicated by the pale gray bonds and
boxed residue labels. The PTPase-WO[4] crystal structure is
indicated by colored bonds and bold residue labels. Coordinates
were superimposed based on the positions of the anion, the
nucleophile, and the guanidinium groups of the arginines. Both
enzymes catalyze hydrolysis of phosphomonoesters and must
stabilize charges at the nucleophile, the PO[3] moiety, and the
leaving group.
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