2MUU
The Proteolytic Activity of Ubiquitin-specific Protease 28 Is Modulated by the N-terminal Domain
Summary for 2MUU
| Entry DOI | 10.2210/pdb2muu/pdb |
| NMR Information | BMRB: 19077 |
| Descriptor | Ubiquitin carboxyl-terminal hydrolase 28 (1 entity in total) |
| Functional Keywords | hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus, nucleoplasm : Q96RU2 |
| Total number of polymer chains | 1 |
| Total formula weight | 14562.97 |
| Authors | |
| Primary citation | Wen, Y.,Shi, L.,Ding, Y.,Cui, R.,He, W.T.,Hu, H.Y.,Zhang, N. The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights. Biochem.J., 471:155-165, 2015 Cited by PubMed Abstract: The deubiquitinase ubiquitin-specific protease 28 (Usp28) contains a ubiquitin-binding region (UBR) composed of one ubiquitin-associated domain (UBA) and one ubiquitin-interacting motif (UIM) at its N-terminus. It is of interest that an additional small ubiquitin-like modifier (SUMO)-interacting motif (SIM) is located next to its UIM. To date, the functional role of the Usp28 UBR is still not understood. To elucidate the regulatory mechanism of the UBR on the full functional display of Usp28, in the present study, NMR and biochemical approaches were applied. The solution structure of Usp28 UBR was obtained, and the key residues responsible for ubiquitin and SUMO1/2 recognition were identified. In addition, we find that the ubiquitin-binding ability of Usp28 UBR was required for full enzymatic activity of Usp28, whereas binding of SUMO1/2 impaired the catalytic activity of the enzyme by competitively blocking its interactions with ubiquitin substrates. Our findings provide a first insight into understanding how the enzymatic activity of Usp28 is regulated by its non-catalytic UBR and endogenous ligands. PubMed: 26268556DOI: 10.1042/BJ20150088 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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