Extended Data Fig. 6: Glycosylation stabilizes substrate-enzyme interactions.
From: O-GlcNAcylation promotes pancreatic tumor growth by regulating malate dehydrogenase 1
a, The residue root-mean-square fluctuation (RMSF) of pMDH1. The difference is the RMSF value of nonglycosylated simulations minus the RMSF value of the glycosylated simulations. A positive value indicates a residue is more rigid with S189 glycosylation while a negative value indicates a residue is more flexible. b, Comparison of the interaction network (contact probability) between MDH1 with NADH (left), and MDH1 with MAK (right) of WT (top) and MDH1 with glycosylated S189 (bottom). Only the residues with a probability of more than 10% are shown. c, The overall average contact probabilities between NADH and MAK of WT (left) MDH1 with glycosylated S189 (right). d, The snapshot of the interaction network between substrates and glycosylated S189. e, The contact probability between GlcNAc and all residues of MDH1, and a schematic diagram to show the major contact residues. f, Relative enzymatic activity of WT or the triplet mutant of MDH1 in the presence or absence of OGT overexpression (n = 5 independent assays). Error bars of data in f denote the means ± SD. Statistical analyses were performed by two-tailed Student’s t-test.
