Figure 3 - full size

 

Figure 3.
FIGURE 3. a, superposition of the protein backbones for apo-PMM/PGM (Apo) and its complexes with G16P. DP, dephospho-PMM/PGM; P, phospho-PMM/PGM. Domains 1–4 are shown in green, yellow, red, and blue, respectively. G16P as bound to phosphoenzyme is shown in magenta and to dephosphoenzyme is shown in cyan. b, a close-up view of G16P in the active site of the two PMM/PGM-intermediate complexes showing their different relative binding positions. The protein backbone is shown in solid (dephosphoenzyme) and semitransparent (phosphoenzyme). Shown are hydrogen bonds between G16P and dephospho-PMM/PGM (c) and phospho-PMM/PGM (d). Protein residues that contact the intermediate are shown as sticks; water molecules are shown as blue spheres.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 15564-15571) copyright 2006.