Processive Pectin Methylesterases: The Role of Electrostatic Potential, Breathing Motions and Bond Cleavage in the Rectification of Brownian Motions
Figure 6
Cα-Cα distances between the residues Arg267 and Asp143 (red) and Trp317 and Lys223 (black) located at the opposite ends of the Ec-PME binding groove.
The graph shows the distances for the simulation where a full sliding of the oligosaccharide along the binding groove is reported. In such a case, correlated motions of the two flanking regions (see also figure 3) are observed along the binding groove and contribute to the docking of a fresh methylesterified monosaccharide residue into the active site of the protein.
