5JKN
Crystal structure of deubiquitinase MINDY-1
Summary for 5JKN
| Entry DOI | 10.2210/pdb5jkn/pdb |
| Descriptor | Protein FAM63A, DI(HYDROXYETHYL)ETHER, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, cysteine protease, isopeptidase and ubiquitin binding |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 32439.90 |
| Authors | Abdul Rehman, S.A.,Kulathu, Y. (deposition date: 2016-04-26, release date: 2016-06-22, Last modification date: 2024-05-01) |
| Primary citation | Abdul Rehman, S.A.,Kristariyanto, Y.A.,Choi, S.Y.,Nkosi, P.J.,Weidlich, S.,Labib, K.,Hofmann, K.,Kulathu, Y. MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes. Mol.Cell, 63:146-155, 2016 Cited by PubMed Abstract: Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrates to regulate the functional outcome of ubiquitylation. Here we report the discovery of a new family of DUBs, which we have named MINDY (motif interacting with Ub-containing novel DUB family). Found in all eukaryotes, MINDY-family DUBs are highly selective at cleaving K48-linked polyUb, a signal that targets proteins for degradation. We identify the catalytic activity to be encoded within a previously unannotated domain, the crystal structure of which reveals a distinct protein fold with no homology to any of the known DUBs. The crystal structure of MINDY-1 (also known as FAM63A) in complex with propargylated Ub reveals conformational changes that realign the active site for catalysis. MINDY-1 prefers cleaving long polyUb chains and works by trimming chains from the distal end. Collectively, our results reveal a new family of DUBs that may have specialized roles in regulating proteostasis. PubMed: 27292798DOI: 10.1016/j.molcel.2016.05.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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