5lvv | pdb_00005lvv

Human OGT in complex with UDP and fused substrate peptide (Tab1)

spinqualitylabelsall models 5lvv, resolution 2.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lvv is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG, UDP Gene: OGT (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.,Rafie K, Raimi O, Ferenbach AT, Borodkin VS, Kapuria V, van Aalten DMF Open Biol. 2017 Jun;7(6). pii: 170078. doi: 10.1098/rsob.170078. PMID:28659383 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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