2Y4W

Solution structure of human ubiquitin conjugating enzyme Rad6b

2Y4W の概要

• エントリーDOI: 10.2210/pdb2y4w/pdb
• 関連するPDBエントリー: 1JAS 1NXA 2Y43
• NMR情報: BMRB: 17443
• 分子名称: UBIQUITIN-CONJUGATING ENZYME E2 B (1 entity in total)
• 機能のキーワード: ligase, dna damage, dna repair, ubiquitination
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cell membrane (By similarity): P63146
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17328.28

構造登録者

Huang, A.,Hibbert, R.G.,deJong, R.N.,Das, D.,Sixma, T.K.,Boelens, R. (登録日: 2011-01-11, 公開日: 2011-05-11, 最終更新日: 2024-05-15)

主引用文献

Huang, A.,Hibbert, R.G.,Dejong, R.N.,Das, D.,Sixma, T.K.,Boelens, R.
Symmetry and Asymmetry of the Ring-Ring Dimer of Rad18
J.Mol.Biol., 410:424-, 2011

PubMed Abstract: The human ubiquitin-conjugating enzyme Rad6 (E2), with ubiquitin ligase enzyme Rad18 (RING E3), monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Here, we determine the structure of the homodimeric Rad18 RING domains by X-ray crystallography and classify it to RING-RING dimers that dimerize through helices adjacent to the RING domains and through the canonical RING domains. Using NMR spectroscopy and site-directed mutagenesis, we demonstrate that the Rad6b binding site, for the Rad18 RING domain, strongly resembles that of other E2/E3 RING/U-box complexes. We show that the homodimeric Rad18 RING domain can recruit two Rad6b E2 enzymes, whereas the full-length Rad18 homodimer binds only to a single Rad6b molecule. Such asymmetry is a common feature of RING-RING heterodimers and has been observed for the CHIP U-box homodimer. We propose that asymmetry may be a common feature of dimeric RING E3 ligases.

PubMed: 21549715
DOI: 10.1016/J.JMB.2011.04.051

実験手法

SOLUTION NMR