 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](hv5062fig3mag.jpg)
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Figure 3
(a) The suggested reaction mechanism for the 10-FTHFD hydrolase step. For clarity, only N10 and the formyl group of the 10-formyl-THF substrate are shown. The water activated by Asp142 attacks the carbon of the formyl group, generating a tetrahedral intermediate stabilized on the one hand by His106 and on the other hand by Asp142. The end products of this reaction are THF and formate. (b) A comparison of the liganded 10-FTHFD (green C atoms) and human GART (pink C atoms) complexed with a substrate analogue, 10-formyl-5,8,10-trideazafolate. His106 and Asp142 are in an identical conformation and two water molecules in the 10-FTHFD complex superimposing with the O atoms of the hydrated formyl group, Wat227 and Wat266, most likely correspond to the positions of the two reactive O atoms during the hydrolase reaction. |
![[Figure 3]](hv5062fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
