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![[Figure 4]](dw5173fig4mag.jpg)
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Figure 4
The AoAA13-G3(α1,4)G1(α1,6) structure. (a) The AoAA13-G3(α1,4)G1(α1,6) structure (yellow) and a symmetry-related molecule (white) with the His brace (coloured according to molecule) shown as sticks. The active-site Zn is shown as a sphere (grey). The glucosyl-maltotriose ligand is bound in between the two molecules. (b) The His brace is shown in a native conformation (70% occupancy) and in an alternative conformation (30% occupancy) as modelled in the final structure. The maps shown are 2Fo − Fc (blue) and Fo − Fc (green for positive and red for negative) difference maps from a model with fully occupied His91A only, and are contoured at 1.0σ and ±3.0σ, respectively. As shown, modelling a fully occupied native conformation leads to negative difference map density near the active-site metal and positive difference map density near Phe166. (c) Electron density for glucosyl-maltotriose calculated prior to incorporation of the ligand. The 2Fo − Fc (blue) and Fo − Fc (green) maps are shown at contour levels of 0.7σ and 2.5σ, respectively. (d) Glucosyl-maltotriose interactions with AoAA13 (yellow) and a symmetry-related molecule (white). Principal direct interactions are formed through Gln82, Gln141 and Thr194 to Glc1 and Glc3. |
![[Figure 4]](dw5173fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
