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![[Figure 4]](mh5163fig4mag.jpg)
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Figure 4
Superimposition of residue side chains in the active site for apo zNt-FDH and the zNt-FDH–THF and zNt-FDH–10-FDDF complexes. (a) zNt-FDH surface structure with 10-FDDF and THF bound in the active site. (b) A stereoview of conformational changes in the active site between the apo form and the 10-FDDF and THF complexes. 10-FDDF (orange) and THF (yellow) are shown in ball-and-stick representation. Residues of zNt-FDH (green), the 10-FDDF complex (magenta) and the THF complex (cyan) are shown as stick representations. The three loops 86–90, 135–143 and 200–203 are closed to the binding cavity with the product THF and substrate 10-FDDF bound. In the structure of THF-bound zNt-FDH, the conformation of the side chain of Tyr200 rotates by 90° to facilitate product binding. |
![[Figure 4]](mh5163fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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