5LWV

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

5LWV の概要

• エントリーDOI: 10.2210/pdb5lwv/pdb
• 分子名称: Host cell factor 1,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, URIDINE-5'-DIPHOSPHATE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: glycosylation, signalling, o-glcnac, o-glcnac transferase, substrate recognition, transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Isoform 2: Mitochondrion. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: O15294
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 84465.59

構造登録者

Raimi, O.,Rafie, K.,Kapuria, V.,Herr, W.,van Aalten, D. (登録日: 2016-09-19, 公開日: 2017-07-12, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)