Skip to main content
. 2015 May 20;290(28):17096–17105. doi: 10.1074/jbc.M115.657866

FIGURE 5.

FIGURE 5.

Structure of the reduced ASC. A, close-up view of the cross-linking site in the ASC, colored as in Fig. 3C. B, close-up view of the cross-linking site in the reduced ASC. Protein and DNA are in pink. C, protein superposition of panels A and B. D, exo-site in the ASC, colored as in Fig. 2B. Important hydrogen-bonding interactions between the protein and the cytosine are denoted in dotted lines, with the associated numbers, showing distances in Å. E, exo-site in the reduced ASC, colored as in panel B. F, protein superposition of panels D and E. G, superposition of the wild-type protein in the abasic site complex (PDB ID: 1RRS) with the protein in the ASC. The wild-type protein (with Pro-164) and the DNA in ASC are shown. H, superposition of panels D and G. The σA-weighted 2Fo − Fc map is contoured at 1σ in panels A, B, and E. The Fo − Fc map is contoured at 3σ in panels A and B and at 2.5σ in panel E.