4GZ3

Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide

Summary for 4GZ3

• Entry DOI: 10.2210/pdb4gz3/pdb
• Related: 4GYW 4GYY 4GZ5 4GZ6
• Descriptor: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, Casein kinase II subunit alpha, URIDINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: ogt, o-glcnac, gt-b, glycosyltransferase, o-glcnacylation, transferase-peptide complex, transferase/peptide
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 166317.20

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: 2024-10-16)

Primary citation

Lazarus, 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

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)