Rafie, Karim Raimi, Olawale Ferenbach, Andrew T. Borodkin, Vladimir S. Kapuria, Vaibhav M. F. van Aalten, Daan Figure S1 from Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats O-linked <i>N</i>-acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-GlcNAc proteome, it is not understood how it recognizes its protein substrates, targeting only a fraction of serines/threonines in the metazoan proteome for glycosylation. We describe a trapped complex of human OGT with the C-terminal domain of TAB1, a key innate immunity signalling O-GlcNAc protein, revealing extensive interactions with the tetratricopeptide repeats of OGT. Confirmed by mutagenesis, this interaction suggests that glycosylation substrate specificity is achieved by recognition of a degenerate sequon in the active site combined with an extended conformation C-terminal of the O-GlcNAc target site. glycosylation;signalling;O-GlcNAc;O-GlcNAc transferase;substrate recognition 2017-06-15
    https://rs.figshare.com/articles/journal_contribution/Figure_S1_from_Recognition_of_a_glycosylation_substrate_by_the_O-GlcNAc_transferase_TPR_repeats/5110273
10.6084/m9.figshare.5110273.v1