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Figure 1
Overall structure of pro-pap-RSS. (a) Structural overview of pro-pap-RSS-C25mA represented as a cartoon diagram. The pro-domain part of the pro-segment is represented in deep magenta, while the extended pro-peptide part blocking the catalytic cleft is represented in cyan and the rest of the extended loop connecting the mature part is represented in light pink. The L-domain and R-domain of the mature segment are represented in blue and green, respectively. The catalytic residues Cys25mA and His159m are represented as spheres. (b) A plot of the average B factor against residue number of the protein. The region within the two arrows represents the high-B-factor residues (87p–107p) of the extended loop of the pro-segment connecting the mature part (light pink region of the cartoon diagram). (c) A representative section of electron-density map (2Fo − Fc) contoured at 1.2σ. (d) Superposition of the Cα traces of pro-pap-RSS-C25mA (black), pro-caricain (light green) and pro-cathepsins L (yellow), K (blue) and S (magenta). |