4WLG

crystal structure of mouse Xyloside xylosyltransferase 1, apo form

4WLG の概要

• エントリーDOI: 10.2210/pdb4wlg/pdb
• 関連するPDBエントリー: 4WLM 4WLZ 4WM0 4WMA 4WMB
• 分子名称: Xyloside xylosyltransferase 1, SULFATE ION (2 entities in total)
• 機能のキーワード: glycosyltransferase, apo from, transferase
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Endoplasmic reticulum membrane ; Single-pass type II membrane protein : Q3U4G3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71071.32

構造登録者

Yu, H.,Li, H. (登録日: 2014-10-07, 公開日: 2015-11-04, 最終更新日: 2024-10-30)

主引用文献

Yu, H.,Takeuchi, M.,LeBarron, J.,Kantharia, J.,London, E.,Bakker, H.,Haltiwanger, R.S.,Li, H.,Takeuchi, H.
Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism.
Nat.Chem.Biol., 11:847-854, 2015

PubMed Abstract: A major question remaining in glycobiology is how a glycosyltransferase (GT) that retains the anomeric linkage of a sugar catalyzes the reaction. Xyloside α-1,3-xylosyltransferase (XXYLT1) is a retaining GT that regulates Notch receptor activation by adding xylose to the Notch extracellular domain. Here, using natural acceptor and donor substrates and active Mus musculus XXYLT1, we report a series of crystallographic snapshots along the reaction, including an unprecedented natural and competent Michaelis reaction complex for retaining enzymes. These structures strongly support the SNi-like reaction as the retaining mechanism for XXYLT1. Unexpectedly, the epidermal growth factor-like repeat acceptor substrate undergoes a large conformational change upon binding to the active site, providing a structural basis for substrate specificity. Our improved understanding of this retaining enzyme will accelerate the design of retaining GT inhibitors that can modulate Notch activity in pathological situations in which Notch dysregulation is known to cause cancer or developmental disorders.

PubMed: 26414444
DOI: 10.1038/nchembio.1927

実験手法

X-RAY DIFFRACTION (3 Å)