journal menu
![[Figure 4]](ag5030fig4mag.jpg)
|
|
Figure 4
Ternary-complex structures of the Y128F mutant. (a) The Y128F mutant soaked with benzoylformate, which mainly adopts a pro-R conformation. (b) The Y128F mutant liganded with benzoate, which is the product of the four-electron oxidation reaction catalyzed by the Y128F mutant in the presence of (S)-mandelate. (c) The Y128F mutant liganded with phenylpyruvate, an oxidized product, when soaked with phenyllactate. (d) The Y128F mutant liganded with phenylacetate, which is the product of the four-electron oxidation reaction catalyzed by the Y128F mutant in the presence of 2-phenyllactate. (e) Y128F bound by the α-hydroxylacid analog 2-hydroxypropanoate. (f) When the Y128F mutant is bound by (R)-mandelate, the structural conformation is similar to that of (S)-mandelate, while the α-OH group points away from His252. The free ligands, FMN and active-site residues are shown in cyan, yellow and green, respectively. The 2Fo − Fc electron-density map is contoured at 2σ. |
![[Figure 4]](ag5030fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
