Figure 6
From: Alanine substitution in cellobiohydrolase provides new insights into substrate threading
Comparison of the interactions of N62 and subsite −4 with that of N222 and subsite −4 in WT simulations. (a) Subsites −3 to −5 and three residues near the location: N62, W63, and N222. (b) Histograms of the dihedral angle (N–Cα–Cβ–Cγ) of N62 in substrate threading (black solid) and occupied (dashed grey) simulations, and (c) the same histograms for N222 (similar colours). (d) Typical conformation of the major frequency with a dihedral angle of 309° (approx. 300°) for N62 (1st, 77.2 ns). (e) Free energy landscapes of substrate threading in WT and the N62A mutant. Binding free energy of the cellulose substrate with WT (blue) or N62A (red) mutant at each subsite was calculated using the MM/GBSA method. Error bar: Standard error.
