4GYW

Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide

4GYW の概要

• エントリーDOI: 10.2210/pdb4gyw/pdb
• 関連するPDBエントリー: 4GYY 4GZ3 4GZ5 4GZ6
• 分子名称: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, Casein kinase II subunit alpha, URIDINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: gt-b, glycosyltransferase, glcnacylation, transferase-peptide complex, transferase/peptide
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 166285.07

構造登録者

Lazarus, M.B.,Jiang, J.,Gloster, T.M.,Zandberg, W.F.,Vocadlo, D.J.,Walker, S. (登録日: 2012-09-05, 公開日: 2012-10-31, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)