4I1F
Structure of Parkin-S223P E3 ligase
Summary for 4I1F
| Entry DOI | 10.2210/pdb4i1f/pdb |
| Related | 4I1H |
| Descriptor | E3 ubiquitin-protein ligase parkin, ZINC ION, BARIUM ION, ... (4 entities in total) |
| Functional Keywords | rbr e3 ubiquitin ligase, ligase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cytosol: O60260 |
| Total number of polymer chains | 1 |
| Total formula weight | 37109.25 |
| Authors | Lougheed, J.C.,Brecht, E.,Yao, N.H. (deposition date: 2012-11-20, release date: 2013-06-19, Last modification date: 2024-11-20) |
| Primary citation | Riley, B.E.,Lougheed, J.C.,Callaway, K.,Velasquez, M.,Brecht, E.,Nguyen, L.,Shaler, T.,Walker, D.,Yang, Y.,Regnstrom, K.,Diep, L.,Zhang, Z.,Chiou, S.,Bova, M.,Artis, D.R.,Yao, N.,Baker, J.,Yednock, T.,Johnston, J.A. Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases. Nat Commun, 4:1982-1982, 2013 Cited by PubMed Abstract: Parkin is a RING-between-RING E3 ligase that functions in the covalent attachment of ubiquitin to specific substrates, and mutations in Parkin are linked to Parkinson's disease, cancer and mycobacterial infection. The RING-between-RING family of E3 ligases are suggested to function with a canonical RING domain and a catalytic cysteine residue usually restricted to HECT E3 ligases, thus termed 'RING/HECT hybrid' enzymes. Here we present the 1.58 Å structure of Parkin-R0RBR, revealing the fold architecture for the four RING domains, and several unpredicted interfaces. Examination of the Parkin active site suggests a catalytic network consisting of C431 and H433. In cells, mutation of C431 eliminates Parkin-catalysed degradation of mitochondria, and capture of an ubiquitin oxyester confirms C431 as Parkin's cellular active site. Our data confirm that Parkin is a RING/HECT hybrid, and provide the first crystal structure of an RING-between-RING E3 ligase at atomic resolution, providing insight into this disease-related protein. PubMed: 23770887DOI: 10.1038/ncomms2982 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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