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5D2M

Complex between human SUMO2-RANGAP1, UBC9 and ZNF451

Summary for 5D2M
Entry DOI10.2210/pdb5d2m/pdb
DescriptorSUMO-conjugating enzyme UBC9, Small ubiquitin-related modifier 2, Ran GTPase-activating protein 1, ... (6 entities in total)
Functional Keywordscomplex, sumo, e3 ligase, ligase, protein binding
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains7
Total formula weight99999.93
Authors
Cappadocia, L.,Lima, C.D. (deposition date: 2015-08-05, release date: 2015-11-04, Last modification date: 2024-11-20)
Primary citationCappadocia, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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