2MT6

Solution structure of the human ubiquitin conjugating enzyme Ube2w

2MT6 の概要

• エントリーDOI: 10.2210/pdb2mt6/pdb
• NMR情報: BMRB: 25150
• 分子名称: Ubiquitin-conjugating enzyme E2 W (1 entity in total)
• 機能のキーワード: ubiquitin, ube2w, e2, ubiquitin conjugating enzyme, ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : Q96B02
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17350.85

構造登録者

Vittal, V.,Shi, L.,Wenzel, D.M.,Brzovic, P.S.,Klevit, R.E. (登録日: 2014-08-14, 公開日: 2014-11-26, 最終更新日: 2024-05-01)

主引用文献

Vittal, V.,Shi, L.,Wenzel, D.M.,Scaglione, K.M.,Duncan, E.D.,Basrur, V.,Elenitoba-Johnson, K.S.,Baker, D.,Paulson, H.L.,Brzovic, P.S.,Klevit, R.E.
Intrinsic disorder drives N-terminal ubiquitination by Ube2w.
Nat.Chem.Biol., 11:83-89, 2015

PubMed Abstract: Ubiquitination of the αN-terminus of protein substrates has been reported sporadically since the early 1980s. However, the identity of an enzyme responsible for this unique ubiquitin (Ub) modification has only recently been elucidated. We show the Ub-conjugating enzyme (E2) Ube2w uses a unique mechanism to facilitate the specific ubiquitination of the α-amino group of its substrates that involves recognition of backbone atoms of intrinsically disordered N termini. We present the NMR-based solution ensemble of full-length Ube2w that reveals a structural architecture unlike that of any other E2 in which its C terminus is partly disordered and flexible to accommodate variable substrate N termini. Flexibility of the substrate is critical for recognition by Ube2w, and either point mutations in or the removal of the flexible C terminus of Ube2w inhibits substrate binding and modification. Mechanistic insights reported here provide guiding principles for future efforts to define the N-terminal ubiquitome in cells.

PubMed: 25436519
DOI: 10.1038/nchembio.1700

実験手法

SOLUTION NMR