%0 Journal Article %A Rafie, Karim %A Raimi, Olawale %A Ferenbach, Andrew T. %A Borodkin, Vladimir S. %A Kapuria, Vaibhav %A M. F. van Aalten, Daan %D 2017 %T Figure S2 from Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats %U https://rs.figshare.com/articles/journal_contribution/Figure_S2_from_Recognition_of_a_glycosylation_substrate_by_the_O-GlcNAc_transferase_TPR_repeats/5110270 %R 10.6084/m9.figshare.5110270.v1 %2 https://ndownloader.figshare.com/files/8675161 %K glycosylation %K signalling %K O-GlcNAc %K O-GlcNAc transferase %K substrate recognition %X O-linked N-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. %I The Royal Society