10.6084/m9.figshare.5110273.v1
Karim Rafie
Karim
Rafie
Olawale Raimi
Olawale
Raimi
Andrew T. Ferenbach
Andrew T.
Ferenbach
Vladimir S. Borodkin
Vladimir S.
Borodkin
Vaibhav Kapuria
Vaibhav
Kapuria
Daan M. F. van Aalten
Daan
M. F. van Aalten
Figure S1 from Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats
The Royal Society
2017
glycosylation
signalling
O-GlcNAc
O-GlcNAc transferase
substrate recognition
2017-06-15 05:31:54
Journal contribution
https://rs.figshare.com/articles/journal_contribution/Figure_S1_from_Recognition_of_a_glycosylation_substrate_by_the_O-GlcNAc_transferase_TPR_repeats/5110273
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.