Figure 2
(a) The C-terminal residues of protomer D (crystal form II), corresponding to the P6–P1 autoprocessed site of the mature enzyme fitted to the mFo − DFc electron-density maps shown (contour level of 3.0σ, green; 1.55 Å resolution) after a round of refinement with the C-terminal residues omitted from the model. (b) Illustration of the binding of the C-terminal tail (spheres) of protomer D (magenta ribbons) to the homodimer formed by protomer A (gray surface) and protomer B (cyan surface). |