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![[Figure 1]](ji5007fig1mag.jpg)
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Figure 1
(a) Distorted tetrahedral coordination of zinc in StPMI. The image was drawn using ChemDraw Professional 15. (b) Site of mutation in the H99A (left), E134A (centre) and H255A (right) mutants. Superposed residues from the wild-type protein (PDB entry 3h1m) are shown in green, while those of the mutants are shown in blue, orange and purple, respectively. The 2Fo − Fc map was contoured at 1.0σ. No blob of density was found in the maps corresponding to the mutants at the site of the bound zinc ion (grey sphere) in the wild-type protein. In the H99A and H255A mutants, water molecules close to the zinc-binding site are shown as red spheres. In the E134A mutant, a molecule of ethylene glycol (EDO-1), shown in stick representation, could be fitted to the density observed close to the zinc-binding site. Hydrogen bonds are shown as dashed lines with bond distances (in Å) given above them. (c) Activity assay for the wild type (WT) and alanine mutants of the zinc-binding residues. The y axis has been intercepted to accommodate the activity of wild-type StPMI. The values represent measurements from two independent batches of purified protein. |
![[Figure 1]](ji5007fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
