Figure 1

The overall architecture of 11S globulin from Wrightia tinctoria. (A) The stereoview of the two-fold axis of symmetry of WTG hexamer. The X1-Y1 axis represents the two-fold axis of symmetry between the two trimers of WTG. The X2-Y2 axis represents the threefold axis of symmetry present in the trimers of WTG. The IA and IE surfaces of the trimers have been indicated by red arrows. All the chains of the WTG hexamer are represented in cartoon form. Six monomers are shown in blue (chain A), green (chain B), cyan (chain C), yellow (chain D), red (chain E), and orange (chain F). (B) The WTG monomer depicting acidic subunit (blue) and basic subunit (green) having 26 β-sheets and 8 α-helices. The Gly285 asparaginyl endopeptidase cleavage site, intra-subunit (Cys44-Cys77) and inter-subunit (Cys120-Cys291) disulphide bonds are represented as ball-and-stick. The extended alpha helix and bicupin fold have been indicated. (C) The stereoview of the three-fold axis of symmetry of WTG trimer from the top. The triangle represents the axis perpendicular to the three-fold axis of symmetry. (D) The electrostatic surface potential of intra-subunit (IA) surface of trimer ABC in the presence and absence of Ser27-Ser34 residues, respectively. The region covers the hydrophilic channel formed at the center of the trimer (yellow box).