3TMO
The catalytic domain of human deubiquitinase DUBA
Summary for 3TMO
| Entry DOI | 10.2210/pdb3tmo/pdb |
| Related | 3TMP |
| Descriptor | OTU domain-containing protein 5 (2 entities in total) |
| Functional Keywords | otu fold, deubiquitinase, phosphorylation, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 21598.61 |
| Authors | Yin, J.,Bosanac, I.,Ma, X.,Hymowitz, S.,Starovasnik, M.,Cochran, A. (deposition date: 2011-08-31, release date: 2012-01-11, Last modification date: 2024-11-20) |
| Primary citation | Huang, O.W.,Ma, X.,Yin, J.,Flinders, J.,Maurer, T.,Kayagaki, N.,Phung, Q.,Bosanac, I.,Arnott, D.,Dixit, V.M.,Hymowitz, S.G.,Starovasnik, M.A.,Cochran, A.G. Phosphorylation-dependent activity of the deubiquitinase DUBA. Nat.Struct.Mol.Biol., 19:171-175, 2012 Cited by PubMed Abstract: Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly regulated process that contributes to cellular signaling and protein stability. Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. The crystal structure of the ubiquitin aldehyde adduct of active DUBA reveals a marked cooperation between phosphorylation and substrate binding. An intricate web of interactions involving the phosphate and the C-terminal tail of ubiquitin cause DUBA to fold around its substrate, revealing why phosphorylation is essential for deubiquitinase activity. Phosphoactivation of DUBA represents an unprecedented mode of protease regulation and a clear link between two major cellular signal transduction systems: phosphorylation and ubiquitin modification. PubMed: 22245969DOI: 10.1038/nsmb.2206 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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