6M2D
MUL1-RING domain
Summary for 6M2D
| Entry DOI | 10.2210/pdb6m2d/pdb |
| Descriptor | Mitochondrial ubiquitin ligase activator of NFKB 1, ZINC ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | mul1, structural protein, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 6 |
| Total formula weight | 38870.16 |
| Authors | Lee, S.O.,Ryu, K.S.,Chi, S.-W. (deposition date: 2020-02-27, release date: 2021-04-07, Last modification date: 2023-11-29) |
| Primary citation | Lee, M.S.,Lee, S.O.,Choi, J.,Ryu, M.,Lee, M.K.,Kim, J.H.,Hwang, E.,Lee, C.K.,Chi, S.W.,Ryu, K.S. MUL1-RING recruits the substrate, p53-TAD as a complex with UBE2D2-UB conjugate. Febs J., 2022 Cited by PubMed Abstract: The RING domain of MUL1 (RING ) alone mediates ubiquitylation of the p53-transactivation domain (TAD ). To elucidate the mechanism underlying the simultaneous recruitment of UBE2D2 and the substrate TAD by RING , we determined the complex structure of RING :UBE2D2 and studied the interaction between RING and TAD in the presence of UBE2D2-UB thioester (UBE2D2~UB) mimetics. The RING -binding induced the closed conformation of UBE2D2 -UB oxyester (UBE2D2 -UB ), and strongly accelerated its hydrolysis, which was suppressed by the additional N77A-mutation of UBE2D2. Interestingly, UBE2D2 -UB oxyester (UBE2D2 -UB ) already formed a closed conformation in the absence of RING . Although TAD exhibited weak binding for RING or UBE2D2 alone, its binding affinity was enhanced and even further for RING :UBE2D2 and RING :UBE2D2 -UB , respectively. The recognition of TAD by RING as a complex with UBE2D2~UB is related to the multivalency of the binding events and underlies the ability of RING to ubiquitylate the intrinsically disordered protein, TAD . PubMed: 35048531DOI: 10.1111/febs.16360 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.795 Å) |
Structure validation
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