5D2M

Complex between human SUMO2-RANGAP1, UBC9 and ZNF451

5D2M の概要

• エントリーDOI: 10.2210/pdb5d2m/pdb
• 分子名称: SUMO-conjugating enzyme UBC9, Small ubiquitin-related modifier 2, Ran GTPase-activating protein 1, ... (6 entities in total)
• 機能のキーワード: complex, sumo, e3 ligase, ligase, protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 99999.93

構造登録者

Cappadocia, L.,Lima, C.D. (登録日: 2015-08-05, 公開日: 2015-11-04, 最終更新日: 2024-11-20)

主引用文献

Cappadocia, L.,Pichler, A.,Lima, C.D.
Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase.
Nat.Struct.Mol.Biol., 22:968-975, 2015

PubMed Abstract: E3 protein ligases enhance transfer of ubiquitin-like (Ubl) proteins from E2 conjugating enzymes to substrates by stabilizing the thioester-charged E2~Ubl in a closed configuration optimally aligned for nucleophilic attack. Here, we report biochemical and structural data that define the N-terminal domain of the Homo sapiens ZNF451 as the catalytic module for SUMO E3 ligase activity. The ZNF451 catalytic module contains tandem SUMO-interaction motifs (SIMs) bridged by a Pro-Leu-Arg-Pro (PLRP) motif. The first SIM and PLRP motif engage thioester-charged E2~SUMO while the next SIM binds a second molecule of SUMO bound to the back side of E2. We show that ZNF451 is SUMO2 specific and that SUMO modification of ZNF451 may contribute to activity by providing a second molecule of SUMO that interacts with E2. Our results are consistent with ZNF451 functioning as a bona fide SUMO E3 ligase.

PubMed: 26524494
DOI: 10.1038/nsmb.3116

実験手法

X-RAY DIFFRACTION (2.4 Å)