 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](hv5062fig2mag.jpg)
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Figure 2
(a) Binding mode of the ligand in 10-FTHFD. The final refined coordinates for the complex are shown and a difference electron-density map after refinement in the absence of the 6-formyltetrahydropterin ligand (contour level 2.5σ) is superimposed. Polar interactions are indicated by green lines. (b) Conformational changes in 10-FTHFD upon active-site ligand binding. While the conformations of the catalytic residues are identical between the apo (orange) and liganded (green) forms, slight movements of the two loops lining the substrate-binding cavity occur. Specifically, both Leu141 and Phe89 swing in to interact with the pteridyl group via van der Waals forces. (c) Comparison of the surfaces of the apo (left) and liganded (right) structures. Phe89 and Leu141 are indicated by magenta and cyan colours, respectively, and the 6-formyltetrahydropterin surface is shown in yellow. A small loop movement and a change in the side-chain conformations of Phe89 and Leu141 results in the sealing of the surface gap (arrow) seen in the apo structure. |
![[Figure 2]](hv5062fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
