3AXC

Crystal structure of linear diubiquitin

3AXC の概要

• エントリーDOI: 10.2210/pdb3axc/pdb
• 分子名称: Ubiquitin, GLYCEROL (3 entities in total)
• 機能のキーワード: nf kappa b signaling, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Ubiquitin: Cytoplasm : P62979
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17371.88

構造登録者

Rohaim, A.,Kawasaki, M.,Kato, R.,Dikic, I.,Wakatsuki, S. (登録日: 2011-04-01, 公開日: 2012-01-25, 最終更新日: 2023-11-01)

主引用文献

Rohaim, A.,Kawasaki, M.,Kato, R.,Dikic, I.,Wakatsuki, S.
Structure of a compact conformation of linear diubiquitin
Acta Crystallogr.,Sect.D, 68:102-108, 2012

PubMed Abstract: Post-translational modifications involving ubiquitin regulate a wide range of biological processes including protein degradation, responses to DNA damage and immune signalling. Ubiquitin polymerizes into chains which may contain eight different linkage types; the ubiquitin C-terminal glycine can link to one of the seven lysine residues or the N-terminal amino group of methionine in the distal ubiquitin molecule. The latter head-to-tail linkage type, referred to as a linear ubiquitin chain, is involved in NF-κB activation through specific interactions with NF-κB essential modulator (NEMO). Here, a crystal structure of linear diubiquitin at a resolution of 2.2 Å is reported. Although the two ubiquitin moieties do not interact with each other directly, the overall structure adopts a compact but not completely closed conformation with a few intermoiety contacts. This structure differs from the previously reported extended conformation, which resembles Lys63-linked diubiquitin, suggesting that the linear polyubiquitin chain is intrinsically flexible and can adopt multiple conformations.

PubMed: 22281738
DOI: 10.1107/S0907444911051195

実験手法

X-RAY DIFFRACTION (2.19 Å)