2MP2

Solution structure of SUMO dimer in complex with SIM2-3 from RNF4

2MP2 の概要

• エントリーDOI: 10.2210/pdb2mp2/pdb
• NMR情報: BMRB: 19961
• 分子名称: Small ubiquitin-related modifier 3, E3 ubiquitin-protein ligase RNF4 (3 entities in total)
• 機能のキーワード: sumo, dimer, sim, rnf4, complex, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P55854 P55854 Q9QZS2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 22415.96

構造登録者

Xu, Y.,Plechanovov, A.,Simpson, P.,Marchant, J.,Leidecker, O.,Sebastian, K.,Hay, R.T.,Matthews, S.J. (登録日: 2014-05-09, 公開日: 2014-07-02, 最終更新日: 2024-05-01)

主引用文献

Xu, Y.,Plechanovova, A.,Simpson, P.,Marchant, J.,Leidecker, O.,Kraatz, S.,Hay, R.T.,Matthews, S.J.
Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.
Nat Commun, 5:4217-4217, 2014

PubMed Abstract: The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer.

PubMed: 24969970
DOI: 10.1038/ncomms5217

実験手法

SOLUTION NMR