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: 2024-11-20) |
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 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: 26524494DOI: 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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