2CM0

The PUB domain functions as a p97 binding module in human peptide N-glycanase.

2CM0 の概要

• エントリーDOI: 10.2210/pdb2cm0/pdb
• 関連するPDBエントリー: 2CCQ
• 分子名称: PEPTIDE N-GLYCANASE HOMOLOG, DI(HYDROXYETHYL)ETHER, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• 機能のキーワード: transferase, kinase, pug domain
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11099.70

構造登録者

Allen, M.D.,Buchberger, A.,Bycroft, M. (登録日: 2006-05-03, 公開日: 2006-06-28, 最終更新日: 2023-12-13)

主引用文献

Allen, M.D.,Buchberger, A.,Bycroft, M.
The Pub Domain Functions as a P97 Binding Module in Human Peptide N-Glycanase.
J.Biol.Chem., 281:25502-, 2006

PubMed Abstract: The AAA ATPase p97 is a ubiquitin-selective molecular machine involved in multiple cellular processes, including protein degradation through the ubiquitin-proteasome system and homotypic membrane fusion. Specific p97 functions are mediated by a variety of cofactors, among them peptide N-glycanase, an enzyme that removes glycans from misfolded glycoproteins. Here we report the three-dimensional structure of the aminoterminal PUB domain of human peptide N-glycanase. We demonstrate that the PUB domain is a novel p97 binding module interacting with the D1 and/or D2 ATPase domains of p97 and identify an evolutionary conserved surface patch required for p97 binding. Furthermore, we show that the PUB and UBX domains do not bind to p97 in a mutually exclusive manner. Our results suggest that PUB domain-containing proteins constitute a widespread family of diverse p97 cofactors.

PubMed: 16807242
DOI: 10.1074/JBC.M601173200

実験手法

X-RAY DIFFRACTION (1.9 Å)