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![[Figure 2]](ag5031fig2mag.jpg)
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Figure 2
Crystal structures of acyl-FMNred adducts and inhibition mechanism by α-ketoacids. (a) Structures of acyl-FMNred adducts in crystals of the Y128F mutant soaked with benzoylformate (left), phenylpyruvate (center) or oxaloacetate (right). The flavin adducts all are at the si-face of the isoalloxazine ring. (b) LC traces and mass spectra of FMN (i) and phenylacetyl-FMNred (ii). (c, d) Weighted 2Fo − Fc electron-density maps (gray) and unbiased Fo − Fc difference OMIT electron-density maps (blue) for FMN in Hmo (c) and the Y128F mutant (d) without (left) or with a ligand (S-mandelate, center; benzoylformate, right), where the extent of polarization is justified by OMIT electron density (the wild type or Y128F mutant and the absence or presence of a ligand seem to be key factors). The 2Fo − Fc electron-density map is contoured at 2σ; the unbiased Fo − Fc OMIT difference electron-density map is contoured at 4σ. Free ligands, FMN, FMN adducts and active-site residues are colored cyan, yellow, orange and green, respectively. See Supplementary Figs. S3(a), S3(b) and S2(c) for stereoviews and Fo − Fc difference electron-density maps. |
![[Figure 2]](ag5031fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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