1C4Z
STRUCTURE OF AN E6AP-UBCH7 COMPLEX: INSIGHTS INTO THE UBIQUITINATION PATHWAY
Summary for 1C4Z
| Entry DOI | 10.2210/pdb1c4z/pdb |
| Related | 1D5F 1UBQ |
| Descriptor | UBIQUITIN-PROTEIN LIGASE E3A, UBIQUITIN CONJUGATING ENZYME E2 (3 entities in total) |
| Functional Keywords | bilobal structure, elongated shape, e3 ubiquitin ligase, e2 ubiquitin conjugating enzyme, ligase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 142510.89 |
| Authors | Huang, L.,Kinnucan, E.,Wang, G.,Beaudenon, S.,Howley, P.M.,Huibregtse, J.M.,Pavletich, N.P. (deposition date: 1999-10-14, 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 (2.6 Å) |
Structure validation
Download full validation report
