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![[Figure 1]](mh5163fig1mag.jpg)
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Figure 1
The crystal structure and active site of zNt-FDH. (a) The overall structure of the zNt-FDH–THF complex is divided into two subdomains, N-terminal (subdomain 1) and C-terminal (subdomain 2), connected by a long stretch of polypeptide chain. Subdomain 1 contains a six-stranded sheet (parallel β1–β4 and antiparallel β5–β6) and six α-helices. This folate-binding domain constitutes a Rossmann fold, whereas subdomain 2 represents a slightly open β-barrel. Three loops (coloured red) surround the active-site pocket, with superimposed 10-FDDF (orange) and THF (yellow) molecules shown in ball-and-stick representation at the binding position. (b) The molecular surface of apo zNt-FDH is coloured grey and the residues of the catalytic triad, His106, Ser108 and Asp142, are shown in stick representation (green). Hydrogen bonds are presented as black dotted lines with distances indicated. |
![[Figure 1]](mh5163fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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