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![[Figure 3]](mh5163fig3mag.jpg)
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Figure 3
The substrate and products in the active-site pocket of zNt-FDH. (a) Electrostatic surface potential (blue, positive charge; red, negative charge) of the 10-FDDF complex of Nt-FDH. The bound 10-FDDF (orange) is shown in ball-and-stick representation. (b) Interactions between zNt-FDH and 10-FDDF. Hydrogen bonds between residues and between residues and 10-FDDF are presented as black and orange dotted lines, respectively. Two residues (His106 and Asp142) are reported to participate in the catalytic mechanism of both the dehydrogenase and the hydrolase reaction in FDH (Krupenko & Wagner, 1999  ; Krupenko et al., 2001). The ND1 atom of His106 and the OD1 and OD2 atoms of Asp142 interact directly with the OA1 atom of the N10 formyl group. (c) Electrostatic surface potential of the zNt-FDH–THF complex. The bound THF (yellow) is shown in ball-and-stick representation. (d) Interactions between zNt-FDH and THF. Hydrogen bonds between residues and between residues and THF are presented as orange dotted lines. The THF-bound form of zNt-FDH demonstrate that the conformational change of Tyr200 stabilizes the O atom of pABA, such that the –OH group of Tyr200 can directly interact through hydrogen bonding. All of the 2Fo − Fc electron-density maps are contoured at 1.0σ. |
![[Figure 3]](mh5163fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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