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![[Figure 3]](dw5188fig3mag.jpg)
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Figure 3
Active-site view of MtFBPaseII with FBP. (a) The electron-density polder map of F6P indicates strong evidence for the presence of the product in the active site of T84S MtFBPaseII. The figure was prepared with Coot. (b) The structure of apo MtFBPaseII (purple) was superimposed with the structure of the homolog EcFBPaseII (teal) in complex with the substrate FBP. The hydroxyl of Thr84 in wild-type MtFBPaseII and the corresponding hydroxyl in T84S MtFBPaseII superimpose at the same position. The hydrogen bond from Thr90 of EcFBPaseII (corresponding to Thr84 in MtFBPaseII) to FBP (teal) is 3.5 Å in length; Thr84 of MtFPBaseII (purple) is within a 3.8 Å distance of the phosphate group. Gol represents a glycerol molecule. Ca2+ ions are only present in the EcFBPaseII structure, while Mg2+ is present in both structures. |
![[Figure 3]](dw5188fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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