2MP2
Solution structure of SUMO dimer in complex with SIM2-3 from RNF4
Summary for 2MP2
| Entry DOI | 10.2210/pdb2mp2/pdb |
| NMR Information | BMRB: 19961 |
| Descriptor | Small ubiquitin-related modifier 3, E3 ubiquitin-protein ligase RNF4 (3 entities in total) |
| Functional Keywords | sumo, dimer, sim, rnf4, complex, protein binding |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm: P55854 P55854 Q9QZS2 |
| Total number of polymer chains | 3 |
| Total formula weight | 22415.96 |
| Authors | Xu, Y.,Plechanovov, A.,Simpson, P.,Marchant, J.,Leidecker, O.,Sebastian, K.,Hay, R.T.,Matthews, S.J. (deposition date: 2014-05-09, release date: 2014-07-02, Last modification date: 2024-05-01) |
| Primary citation | Xu, Y.,Plechanovova, A.,Simpson, P.,Marchant, J.,Leidecker, O.,Kraatz, S.,Hay, R.T.,Matthews, S.J. Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4. Nat Commun, 5:4217-4217, 2014 Cited by PubMed Abstract: The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer. PubMed: 24969970DOI: 10.1038/ncomms5217 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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