Skip to main content
. Author manuscript; available in PMC: 2020 Feb 1.
Published in final edited form as: Chembiochem. 2018 Nov 12;20(3):312–318. doi: 10.1002/cbic.201800481

Figure 1.

Figure 1.

Overview of O-GlcNAcylation and its cycling enzymes. Top panel: schematic of reversible O-GlcNAcylation. O-GlcNAc cycling enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), are represented by the full-length ncOGT model (generated from PDB 3PE4 and 1W3B) and a truncated human OGA structure (OGAcryst from PDB: 5TKE). Bottom panel: the schematic of domain architecture of ncOGT and OGA. OGT is comprised of a tetratricopeptide repeat domain (TPR, orange), catalytic domain (N-Cat and C-Cat, blue), and intervening domain (Int-D, light gray). OGA is comprised of a catalytic domain (Catalytic, cyan), stalk domain (Stalk, pink), and pseudo-histone acetyltransferase domain (Pseudo HAT, light gray).