1D5F
STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY
Summary for 1D5F
| Entry DOI | 10.2210/pdb1d5f/pdb |
| Related | 1UBQ |
| Descriptor | E6AP HECT CATALYTIC DOMAIN, E3 LIGASE (1 entity in total) |
| Functional Keywords | bilobal structure, elongated shape, e3 ligase, ligase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 3 |
| Total formula weight | 124621.30 |
| Authors | Huang, L.,Kinnucan, E.,Wang, G.,Beaudenon, S.,Howley, P.M.,Huibregtse, J.M.,Pavletich, N.P. (deposition date: 1999-10-07, release date: 1999-11-17, Last modification date: 2024-02-07) |
| Primary citation | Huang, L.,Kinnucan, E.,Wang, G.,Beaudenon, S.,Howley, P.M.,Huibregtse, J.M.,Pavletich, N.P. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science, 286:1321-1326, 1999 Cited by PubMed Abstract: The E6AP ubiquitin-protein ligase (E3) mediates the human papillomavirus-induced degradation of the p53 tumor suppressor in cervical cancer and is mutated in Angelman syndrome, a neurological disorder. The crystal structure of the catalytic hect domain of E6AP reveals a bilobal structure with a broad catalytic cleft at the junction of the two lobes. The cleft consists of conserved residues whose mutation interferes with ubiquitin-thioester bond formation and is the site of Angelman syndrome mutations. The crystal structure of the E6AP hect domain bound to the UbcH7 ubiquitin-conjugating enzyme (E2) reveals the determinants of E2-E3 specificity and provides insights into the transfer of ubiquitin from the E2 to the E3. PubMed: 10558980DOI: 10.1126/science.286.5443.1321 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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