5KY4

mouse POFUT1 in complex with mouse Notch1 EGF26 and GDP

5KY4 の概要

• エントリーDOI: 10.2210/pdb5ky4/pdb
• 関連するPDBエントリー: 5KXH 5KXQ 5KY0 5KY2 5KY3 5KY5 5KY7 5KY8 5KY9
• 分子名称: GDP-fucose protein O-fucosyltransferase 1, Neurogenic locus notch homolog protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: glycosyltransferase, transferase
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45775.73

構造登録者

Li, Z.,Rini, J.M. (登録日: 2016-07-21, 公開日: 2017-05-17, 最終更新日: 2024-11-20)

主引用文献

Li, Z.,Han, K.,Pak, J.E.,Satkunarajah, M.,Zhou, D.,Rini, J.M.
Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1.
Nat. Chem. Biol., 13:757-763, 2017

PubMed Abstract: Protein O-fucosyltransferase 1 (POFUT1) fucosylates the epidermal growth factor (EGF)-like domains found in cell-surface and secreted glycoproteins including Notch and its ligands. Although Notch fucosylation is critical for development, and POFUT1 deficiency leads to human disease, how this enzyme binds and catalyzes the fucosylation of its diverse EGF-like domain substrates has not been determined. Reported here is the X-ray crystal structure of mouse POFUT1 in complex with several EGF-like domains, including EGF12 and EGF26 of Notch. Overall shape complementarity, interactions with invariant atoms of the fucosylation motif and flexible segments on POFUT1 all define its EGF-like-domain binding properties. Using large-scale structural and sequence analysis, we also show that POFUT1 binds EGF-like domains of the hEGF type and that the highly correlated presence of POFUT1 and fucosylatable hEGFs has accompanied animal evolution.

PubMed: 28530709
DOI: 10.1038/nchembio.2381

実験手法

X-RAY DIFFRACTION (1.472 Å)