Three-dimensional structures enolase

Enolase has a complex metal ion requirement,683 69 usually met by Mg2+ and Mn2+. From NMR studies of the relaxation of water protons, it was concluded that a Mn2+ ion coordinates two rapidly exchangeable water molecules in the free enzyme. When substrate binds, one of these water molecules may be immobilized and may participate in an addition reaction that forms phosphoenolpyruvate (reverse of reaction 13-15). A tightly bound "conformational" metal ion is located in the known three-dimensional structure in such a... 

Fig. 4. Modeled three-dimensional structure of C. herbamm enolase. C. herbarum enolase was modeled on the basis of the three-dimensional structure of S. cerevisiae enolase [60, 62], The C. herbarum enolase monomer is shown in magenta, whereas the peptide rCla h6 (120-189) is displayed in blue. Those residues which were predicted to interact with patient IgE are marked. For further explanations, see text. 

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