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4GYY

Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate

Summary for 4GYY
Entry DOI10.2210/pdb4gyy/pdb
Related4GYW 4GZ3 4GZ5 4GZ6
DescriptorUDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, Casein kinase II subunit alpha, (2S,3R,4R,5S,6R)-3-(acetylamino)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-thiopyran-2-yl [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate, ... (5 entities in total)
Functional Keywordsogt, o-glcnac, gt-b, glycosyltransferase, glcnacylation, transferase-peptide complex, transferase/peptide
Biological sourceHomo sapiens (human)
More
Cellular locationIsoform 2: Mitochondrion. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: O15294
Total number of polymer chains4
Total formula weight166281.17
Authors
Lazarus, M.B.,Jiang, J.,Gloster, T.M.,Zandberg, W.F.,Vocadlo, D.J.,Walker, S. (deposition date: 2012-09-05, release date: 2012-10-31, Last modification date: 2024-02-28)
Primary citationLazarus, M.B.,Jiang, J.,Gloster, T.M.,Zandberg, W.F.,Whitworth, G.E.,Vocadlo, D.J.,Walker, S.
Structural snapshots of the reaction coordinate for O-GlcNAc transferase.
Nat.Chem.Biol., 8:966-968, 2012
Cited by
PubMed Abstract: Visualization of the reaction coordinate undertaken by glycosyltransferases has remained elusive but is critical for understanding this important class of enzyme. Using substrates and substrate mimics, we describe structural snapshots of all species along the kinetic pathway for human O-linked β-N-acetylglucosamine transferase (O-GlcNAc transferase), an intracellular enzyme that catalyzes installation of a dynamic post-translational modification. The structures reveal key features of the mechanism and show that substrate participation is important during catalysis.
PubMed: 23103939
DOI: 10.1038/nchembio.1109
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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