5LWV

Human OGT in complex with UDP and fused substrate peptide (HCF1)

Summary for 5LWV

• Entry DOI: 10.2210/pdb5lwv/pdb
• Descriptor: Host cell factor 1,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, URIDINE-5'-DIPHOSPHATE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: glycosylation, signalling, o-glcnac, o-glcnac transferase, substrate recognition, transferase
• Biological source: Homo sapiens (Human); More
• Cellular location: Isoform 2: Mitochondrion. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: O15294
• Total number of polymer chains: 1
• Total formula weight: 84465.59

Authors

Raimi, O.,Rafie, K.,Kapuria, V.,Herr, W.,van Aalten, D. (deposition date: 2016-09-19, release date: 2017-07-12, Last modification date: 2024-01-17)

Primary citation

Rafie, K.,Raimi, O.,Ferenbach, A.T.,Borodkin, V.S.,Kapuria, V.,van Aalten, D.M.F.
Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.
Open Biol, 7:-, 2017

PubMed Abstract: O-linked -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.

PubMed: 28659383
DOI: 10.1098/rsob.170078

Experimental method

X-RAY DIFFRACTION (1.9 Å)