2G9G

Crystal structure of His-tagged mouse PNGase C-terminal domain

2G9G の概要

• エントリーDOI: 10.2210/pdb2g9g/pdb
• 関連するPDBエントリー: 2G9F
• 分子名称: peptide N-glycanase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: beta-sandwich, hydrolase
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25601.31

構造登録者

Zhou, X.,Zhao, G.,Wang, L.,Li, G.,Lennarz, W.J.,Schindelin, H. (登録日: 2006-03-06, 公開日: 2006-10-24, 最終更新日: 2023-08-30)

主引用文献

Zhou, X.,Zhao, G.,Truglio, J.J.,Wang, L.,Li, G.,Lennarz, W.J.,Schindelin, H.
Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module.
Proc.Natl.Acad.Sci.Usa, 103:17214-17219, 2006

PubMed Abstract: The inability of certain N-linked glycoproteins to adopt their native conformation in the endoplasmic reticulum (ER) leads to their retrotranslocation into the cytosol and subsequent degradation by the proteasome. In this pathway the cytosolic peptide-N-glycanase (PNGase) cleaves the N-linked glycan chains off denatured glycoproteins. PNGase is highly conserved in eukaryotes and plays an important role in ER-associated protein degradation. In higher eukaryotes, PNGase has an N-terminal and a C-terminal extension in addition to its central catalytic domain, which is structurally and functionally related to transglutaminases. Although the N-terminal domain of PNGase is involved in protein-protein interactions, the function of the C-terminal domain has not previously been characterized. Here, we describe biophysical, biochemical, and crystallographic studies of the mouse PNGase C-terminal domain, including visualization of a complex between this domain and mannopentaose. These studies demonstrate that the C-terminal domain binds to the mannose moieties of N-linked oligosaccharide chains, and we further show that it enhances the activity of the mouse PNGase core domain, presumably by increasing the affinity of mouse PNGase for the glycan chains of misfolded glycoproteins.

PubMed: 17088551
DOI: 10.1073/pnas.0602954103

実験手法

X-RAY DIFFRACTION (2 Å)