2DOS
Structural basis for the recognition of Lys48-linked polyubiquitin chain by the Josephin domain of ataxin-3, a putative deubiquitinating enzyme
Summary for 2DOS
| Entry DOI | 10.2210/pdb2dos/pdb |
| Descriptor | Ataxin-3 (1 entity in total) |
| Functional Keywords | deubiquitinating enzyme, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus matrix : P54252 |
| Total number of polymer chains | 1 |
| Total formula weight | 20162.67 |
| Authors | Sumiyoshi, A. (deposition date: 2006-05-03, release date: 2007-05-22, Last modification date: 2024-05-01) |
| Primary citation | Satoh, T.,Sumiyoshi, A.,Yagi-Utsumi, M.,Sakata, E.,Sasakawa, H.,Kurimoto, E.,Yamaguchi, Y.,Li, W.,Joazeiro, C.A.,Hirokawa, T.,Kato, K. Mode of substrate recognition by the Josephin domain of ataxin-3, which has an endo-type deubiquitinase activity. Febs Lett., 588:4422-4430, 2014 Cited by PubMed Abstract: Ataxin-3, which is encoded by a gene that has been associated with Machado-Joseph disease, contains a catalytic N-terminal Josephin domain with deubiquitinase activity. Here, we show that the Josephin domain of ataxin 3 catalyzes endo-type cleavage of Lys48-linked polyubiquitin. Furthermore, NMR data obtained following site-specific paramagnetic spin labeling of Lys48-linked di-ubiquitin revealed that both ubiquitin units interact with the Josephin domain, with the C-terminal Gly76 of the proximal unit being situated in the vicinity of the catalytic triad of Josephin domain. Our results help to elucidate how the substrate is recognized by the Josephin domain and properly positioned for an endo-type deubiquitination reaction. PubMed: 25448680DOI: 10.1016/j.febslet.2014.10.013 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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