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Figure 2
β-Mercapto­ethanol- or gluta­thione-adduct Cys777 residue of TLR15TIR. (a) An electron-density map (gray meshes; 3.0σ in FoFc OMIT map) for the β-mercapto­ethanol-adduct Cys777 residue (carbon, light blue; oxygen, red; nitro­gen, blue; sulfur, yellow) in the TLR15TIR structure. (b) An electron-density map (gray meshes; 3.0σ in FoFc OMIT map) for the gluta­thione-adduct Cys777 residue (carbon, magenta; oxygen, red; nitro­gen, blue; sulfur, yellow) in the TLR15TIR-GTT structure. (c) β-Mercapto­ethanol- and gluta­thione-adduct Cys777 residues (light blue and magenta ball-and-stick models, respectively) from the overlaid TLR15TIR and TLR15TIR-GTT structures (gray Cα traces), respectively. (d) Gluta­thione adduct (magenta ball-and-stick model) in the dent of the TLR15TIR-GTT structure (gray surfaces). Gluta­thione consists of Gly, Cys and Glu moieties. (e) Interactions between TLR15 and gluta­thione in the TLR15TIR-GTT structure. The gluta­thione molecule that is linked to TLR15 Cys777 (cyan sticks) is shown as a magenta ball-and-stick model. The gluta­thione-binding residues of TLR15 are depicted as green sticks on gray transparent ribbons representing the TLR15TIR-GTT structure. Hydrogen bonds between gluta­thione and TLR15 residues are represented by black dotted lines.

IUCrJ
Volume 10| Part 3| May 2023| Pages 352-362
ISSN: 2052-2525