Research Article

Three-Dimensional Molecular Modeling of a Diverse Range of SC Clan Serine Proteases

Figure 3

Representative X-ray SC protease structures and modeled SC protease structures from Arabidopsis thaliana and Plasmodium falciparum. Ribbon models of S. scrofa, 1QFS (a), A. pernix, 1VE7 (c), A. thaliana (e), and P. falciparum (g) SC protease structures show β-sheets with an arrow directed to the C-terminus (light blue), α-helices (red and yellow), turn/loops (gray), and catalytic triad residue side chains (green sticks). Surface electrostatic potential models of S. scrofa, 1QFS (b), A. pernix, 1VE7 (d), A. thaliana, PM0078228 (f), and P. falciparum, PM0078229 (h) SC protease structures show electronegative (red), electropositive (blue), and electroneutral (white) amino acid side chains. Electrostatic potential thresholds: −1.4 kT/e < 0.0 kT/e < +1.4 kT/e ( ).
580965.fig.003a
(a)
580965.fig.003b
(b)
580965.fig.003c
(c)
580965.fig.003d
(d)
580965.fig.003e
(e)
580965.fig.003f
(f)
580965.fig.003g
(g)
580965.fig.003h
(h)