Fig. 2
Interactions between GmPOPB and linker regions for 35mer and 25mer substrates are different. a Overview of bound peptides. Colors for distinct peptide regions are as in Fig. 1b, except that the linker in the 25mer complex is in dark gray. Position of the catalytic Ser577, and core and leader proline residues (yellow) are indicated in sticks. b Comparison of the linker region between 35mer (magenta) and 25mer (gray) complexes. Highlighted are the very different position of Glu and His in contrast to tryptophan, which in both structures occupies the same pocket although the conformation is different. c Interactions between peptide tail and linker of the 25mer peptide and GmPOPB-S577A. Residues within hydrogen bonding distance are shown in lines, residues participating in hydrophobic interactions are in spheres, water molecules are depicted as small red spheres, prolines are shown in yellow. Color coding for peptide substrate regions follows a, residues from GmPOPB are depicted in blue. d Interactions between peptide tail, linker, core, and leader (anti-clockwise) of the 35mer peptide and GmPOPB-S577A. The same representation as c is used except residues from GmPOPB are depicted in green
