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Figure 4.
FIGURE 4. Structural changes occurring during the enzyme
reaction. A, close-up view of loops A and B of the wild-type
BiSP covalent intermediate (molecule A; cyan) superimposed on
the glucose product-bound form (molecule B; yellow). The bound
glucose of molecule B is shown for clarity. B, close-up view of
loops A and B and the noncovalently bound glucose molecule of
the wild-type BiSP-glucose complex. Glucose 1-phosphate (yellow)
has been modeled based on the position of the glucose
interacting with Arg^135 and Tyr^344. C, proposed intermolecular
phosphate-binding site created by two Arg^135 residues. The
distances indicated by dashed lines are 3.9 Å. The bound
sucrose molecules are shown as red van der Waals spheres.
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