 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](hv5062fig1mag.jpg)
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Figure 1
(a) Overall structure of human 10-FTHFD. The ligand 6-formyltetrahydropterin is shown as a ball-and-stick model bound to the THF-binding site in the N-terminal domain. The two halves of the folate-binding domain are shown in yellow and green and the two loops covering the binding site in magenta. The C-terminal domain is shown in light blue. (b) Superposition of the human 10-FTHFD with the rat enzyme. The human enzyme is coloured green/blue and the rat enzyme yellow/orange. N-terminal residues up to residue 99 are coloured blue (human) and orange (rat) to illustrate the apparent hinge movement between this region and the rest of the protein. The loop segment acting as a hinge is highlighted by the grey arrow. (c) Structural alignment of human (this study) and rat (Chumanevich et al., 2004  ) 10-FTHFD, E. coli FMT (Gatzeva-Topalova et al., 2005) and human (Dahms et al., 2005) and E. coli (Greasley et al., 1999) GART. The alignment was produced with the SSM server based on structural superposition of the coordinates and includes residues of the folate-binding domain (residues 1–186 in 10-FTHFD). Fully conserved residues are shown on a black background and the secondary-structure elements of human 10-FTHFD are shown above the alignment. Asterisks mark the catalytic residues His106 and Asp142. (d) The domain structure of human 10-FTHFD. |
![[Figure 1]](hv5062fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
