5D2M

Complex between human SUMO2-RANGAP1, UBC9 and ZNF451

Summary for 5D2M

• Entry DOI: 10.2210/pdb5d2m/pdb
• Descriptor: SUMO-conjugating enzyme UBC9, Small ubiquitin-related modifier 2, Ran GTPase-activating protein 1, ... (6 entities in total)
• Functional Keywords: complex, sumo, e3 ligase, ligase, protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 7
• Total formula weight: 99999.93

Authors

Cappadocia, L.,Lima, C.D. (deposition date: 2015-08-05, release date: 2015-11-04, Last modification date: 2023-09-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)