4K7D
Crystal Structure of Parkin C-terminal RING domains
Summary for 4K7D
| Entry DOI | 10.2210/pdb4k7d/pdb |
| Descriptor | E3 ubiquitin-protein ligase parkin, ZINC ION, MALONATE ION, ... (5 entities in total) |
| Functional Keywords | ring domains, zinc fingers, rbr ubiquitin ligase, e3 ubiquitin protein ligase, ubiquitin, ubch7, ligase |
| Biological source | Rattus norvegicus (brown rat,rat,rats) |
| Cellular location | Nucleus (By similarity): Q9JK66 |
| Total number of polymer chains | 3 |
| Total formula weight | 112404.62 |
| Authors | Sauve, V.,Trempe, J.-F.,Menade, M.,Gehring, K. (deposition date: 2013-04-17, release date: 2013-05-15, Last modification date: 2024-02-28) |
| Primary citation | Trempe, J.F.,Sauve, V.,Grenier, K.,Seirafi, M.,Tang, M.Y.,Menade, M.,Al-Abdul-Wahid, S.,Krett, J.,Wong, K.,Kozlov, G.,Nagar, B.,Fon, E.A.,Gehring, K. Structure of parkin reveals mechanisms for ubiquitin ligase activation. Science, 340:1451-1455, 2013 Cited by PubMed Abstract: Mutations in the PARK2 (parkin) gene are responsible for an autosomal recessive form of Parkinson's disease. The parkin protein is a RING-in-between-RING E3 ubiquitin ligase that exhibits low basal activity. We describe the crystal structure of full-length rat parkin. The structure shows parkin in an autoinhibited state and provides insight into how it is activated. RING0 occludes the ubiquitin acceptor site Cys(431) in RING2, whereas a repressor element of parkin binds RING1 and blocks its E2-binding site. Mutations that disrupted these inhibitory interactions activated parkin both in vitro and in cells. Parkin is neuroprotective, and these findings may provide a structural and mechanistic framework for enhancing parkin activity. PubMed: 23661642DOI: 10.1126/science.1237908 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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