6IWR

Crystal structure of GalNAc-T7 with UDP, GalNAc and Mn2+

6IWR の概要

• エントリーDOI: 10.2210/pdb6iwr/pdb
• 分子名称: N-acetylgalactosaminyltransferase 7, MANGANESE (II) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: polypeptide n acetylgalactosaminyltransferase activity, transferring glycosyl groups, manganese ion binding, carbohydrate binding, metal ion binding, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 414747.62

構造登録者

Yu, C.,Yin, Y.X. (登録日: 2018-12-06, 公開日: 2019-02-06, 最終更新日: 2024-11-20)

主引用文献

Yu, C.,Liang, L.,Yin, Y.
Structural basis of carbohydrate transfer activity of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase 7.
Biochem. Biophys. Res. Commun., 510:266-271, 2019

PubMed Abstract: The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) catalyze mucin-type O-glycosylation by transferring α-N-acetylgalactosamine (GalNAc) from UDP- GalNAc to Ser or Thr residues of target proteins. We resolved the crystal structures of GalNAc-T7, a GalNAc-T capable of glycosylating consecutive sites, and of its complex with the donor substrate UDP-GalNAc. The N-terminal catalytic domain and C-terminal lectin domain are connected by a flexible linker, forming a narrow cleft for the acceptor substrate. Only the α subdomain of the lectin domain binds to the glycosyl group, indicating that key residues determine substrate binding. Compared to the Apo structure, the loop covering the catalytic center of the complex show significant conformational changes, indicating the mechanism of the catalytic reaction.

PubMed: 30685086
DOI: 10.1016/j.bbrc.2019.01.084

実験手法

X-RAY DIFFRACTION (2.604 Å)