Figure 2.
Figure 2 PMM/PGM in complex with X1P and R1P. The protein is
colored by domain, with blue, light blue, pink and magenta for
domains 1, 2, 3 and 4, respectively. (a) Ribbon diagram of
PMM/PGM with X1P (yellow) and R1P (green) bound in the active
site. (b) Superposition of the C^ atoms
of the R1P complex with those of apo-PMM/PGM (PDB code 1k2y )
shown in gray, demonstrating the rotation of domain 4. Close-up
view of the active site of PMM/PGM with bound (c) X1P and (d)
R1P. For clarity, only interactions between side chains of the
enzyme and ligands are highlighted; water molecules are shown as
spheres. (e) For comparison, a superposition of the slow
substrate R1P and a preferred substrate G1P (cyan) in the active
site of PMM/PGM is shown.
The above figure is reprinted
by permission from the IUCr:
Acta Crystallograph Sect F Struct Biol Cryst Commun
(2006,
62,
722-726)
copyright 2006.
atoms
of the R1P complex with those of apo-PMM/PGM (PDB code 1k2y )
shown in gray, demonstrating the rotation of domain 4. Close-up
view of the active site of PMM/PGM with bound (c) X1P and (d)
R1P. For clarity, only interactions between side chains of the
enzyme and ligands are highlighted; water molecules are shown as
spheres. (e) For comparison, a superposition of the slow
substrate R1P and a preferred substrate G1P (cyan) in the active
site of PMM/PGM is shown.