Supplementary material from "Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats"
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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.
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Rafie, Karim; Raimi, Olawale; Ferenbach, Andrew T.; Borodkin, Vladimir S.; Kapuria, Vaibhav; M. F. van Aalten, Daan (2017). Supplementary material from "Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats". The Royal Society. Collection. https://doi.org/10.6084/m9.figshare.c.3803632.v2