4LDT

The structure of h/ceOTUB1-ubiquitin aldehyde-UBCH5B~Ub

4LDT の概要

• エントリーDOI: 10.2210/pdb4ldt/pdb
• 分子名称: Ubiquitin thioesterase otubain-like, Ubiquitin aldehyde, Ubiquitin-conjugating enzyme E2 D2, ... (7 entities in total)
• 機能のキーワード: isopeptidase, ubiquitin-conjugating, post-translational modification, ubiquitin, ubiquitin-aldehyde, hydrolase regulator
• 由来する生物種: Homo sapiens (human, nematode); 詳細
• 細胞内の位置: Ubiquitin: Cytoplasm : P0CG48 P0CG48
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67002.09

構造登録者

Wiener, R.,DiBello, A.T.,Lombardi, P.M.,Guzzo, C.M.,Zhang, X.,Matunis, M.J.,Wolberger, C. (登録日: 2013-06-25, 公開日: 2013-08-14, 最終更新日: 2023-12-06)

主引用文献

Wiener, R.,Dibello, A.T.,Lombardi, P.M.,Guzzo, C.M.,Zhang, X.,Matunis, M.J.,Wolberger, C.
E2 ubiquitin-conjugating enzymes regulate the deubiquitinating activity of OTUB1.
Nat.Struct.Mol.Biol., 20:1033-1039, 2013

PubMed Abstract: OTUB1 is a Lys48-specific deubiquitinating enzyme that forms a complex in vivo with E2 ubiquitin (Ub)-conjugating enzymes including UBC13 and UBCH5. OTUB1 binds E2~Ub thioester intermediates and prevents ubiquitin transfer, thereby noncatalytically inhibiting accumulation of polyubiquitin. We report here that a second role of OTUB1-E2 interactions is to stimulate OTUB1 cleavage of Lys48 polyubiquitin. This stimulation is regulated by the ratio of charged to uncharged E2 and by the concentration of Lys48-linked polyubiquitin and free ubiquitin. Structural and biochemical studies of human and worm OTUB1 and UBCH5B show that the E2 enzyme stimulates binding of the Lys48 polyubiquitin substrate by stabilizing folding of the OTUB1 N-terminal ubiquitin-binding helix. Our results suggest that OTUB1-E2 complexes in the cell are poised to regulate polyubiquitin chain elongation or degradation in response to changing levels of E2 charging and available free ubiquitin.

PubMed: 23955022
DOI: 10.1038/nsmb.2655

実験手法

X-RAY DIFFRACTION (1.901 Å)