6K2K
Solution structure of MUL1-RING domain
Summary for 6K2K
| Entry DOI | 10.2210/pdb6k2k/pdb |
| NMR Information | BMRB: 36251 |
| Descriptor | Mitochondrial ubiquitin ligase activator of NFKB 1, ZINC ION (2 entities in total) |
| Functional Keywords | solution structure, e3 ubiquitin ligase, structural protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 6382.30 |
| Authors | |
| Primary citation | Lee, M.S.,Lee, S.O.,Lee, M.K.,Yi, G.S.,Lee, C.K.,Ryu, K.S.,Chi, S.W. Solution structure of MUL1-RING domain and its interaction with p53 transactivation domain. Biochem.Biophys.Res.Commun., 516:533-539, 2019 Cited by PubMed Abstract: Mitochondrial E3 ubiquitin ligase 1 (MUL1) is a multifunctional mitochondrial protein involved in various biological processes such as mitochondrial dynamics, cell growth, apoptosis, and mitophagy. MUL1 mediates the ubiquitylation of mitochondrial p53 for proteasomal degradation. Although the interaction of MUL1-RING domain with its substrate, p53, is a unique mechanism in RING-mediated ubiquitylation, the molecular basis of this process remains unknown. In this study, we determined the solution structure of the MUL1-RING domain and characterized its interaction with the p53 transactivation domain (p53-TAD) by nuclear magnetic resonance (NMR) spectroscopy. The overall structure of the MUL1-RING domain is similar to those of RING domains of other E3 ubiquitinases. The MUL1-RING domain adopts a ββαβ fold with three anti-parallel β-strands and one α-helix, containing a canonical cross-brace motif for the ligation of two zinc ions. Through NMR chemical shift perturbation experiments, we determined the p53-TAD-binding site in the MUL1-RING domain and showed that the MUL1-RING domain interacts mainly with the p53-TAD2 subdomain composed of residues 39-57. Taken together, our results provide a molecular basis for the novel recognition mechanism of the p53-TAD substrate by the MUL1-RING domain. PubMed: 31235254DOI: 10.1016/j.bbrc.2019.06.101 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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