EC Number   |
|---|
   2.3.2.26 | C2 domain, to 1.96 A resolution. The Smurf1 C2 domain possesses a typical anti-parallel beta-sandwich fold. The Smurf1 C2 domain exerts a key role in localization to the plasma membrane. Lysine residues, Lys-28 and Lys-85, within the C2 domain are important for Smurf1 localization at the plasma membrane, regulation on cell migration, and robust ligase activity toward RhoA, which further supports a Ca2+-independent localization mechanism for Smurf1 |
| 2.3.2.26 | crystal structure of a trapped complex of ubiquitin ligase Rsp5 with ubiquitin and substrate Sna3 cytoplasmic domain as a proxy for the catalytic intermediate. The covalent linkage between ubiquitin and the HECT domain is oriented by ubiquitin interactions with the HECT domain N- and C-lobes that stabilize HECT domain conformation. The HECT domain architecture of the ligase primed for ligation prioritizes potential target lysines by their placement relative to a composite catalytic center for ubiquitination |
| 2.3.2.26 | crystal structure of the extended HECT domain of AREL1 (amino acids 436-823) at 2.4 A resolution. The extended HECT domain adopts an inverted, T-shaped, bilobed conformation and harbors an additional loop (aa 567-573) absent in other HECT members. The N-terminal extended region (aa 436-482) preceding the HECT domain is indispensable for its stability and activity and without this region, the HECT domain becomes inactive |
| 2.3.2.26 | crystal structure of the HECT domain of human ubiquitin ligase WWP1/AIP5 maintains a two-lobed structure like the HECT domain of the human ubiquitin ligase E6AP. The organization of the two lobes relative one another is different from E6AP due to a rotation about a polypeptide hinge linking the N and C lobes |
| 2.3.2.26 | crystal structure of the HECT domain of UBE3C (amino acids 744-1083) with an additional fifty N-terminal amino acids (aa 693-743) at 2.7 A. The UBE3C HECT domain forms an open, L-shaped, bilobed conformation, having a large N-lobe and a small C-lobe. The N-terminal region (aa 693-743) preceding the UBE3C HECT domain as well as a loop region (aa 758-762) in the N-lobe of the HECT domain affect the stability and activity of UBE3C HECT domain |
| 2.3.2.26 | hanging drop vapor diffusion method, using 0.1 M HEPES pH 8.4, 0.2 M MgCl2, 15% (v/v) ethanol at 4°C |
| 2.3.2.26 | Huwe1 C-lobe-ubiquitin crystal structure at 2.8 A resolution, by molecular replacement and solution NMR spectroscopy |
| 2.3.2.26 | Smurf2 C-lobe-ubiquitin crystal structure at 2.8 A resolution, by molecular replacement and solution NMR spectroscopy |
| 2.3.2.26 | structure of isoform NleL contains two domains, a beta-helix domain formed by pentapeptide repeats and a bilobed catalytic domain reminiscent of the N- and C-lobe architecture of HECT E3s. The C-lobe adopts a large range of different positions relative to the N-lobe, indicating that the helix linking the two lobes is extremely flexible |
| 2.3.2.26 | structure of ubiquitin-loaded human neural precursor cellexpressed developmentally downregulated protein, Nedd4, to 2.51 A resolution. The Nedd4-HECT domain-ubiquitin transitory intermediate provides a structural basis for the proposed sequential addition mechanism. The donor ubiquitin, transferred from the E2, is bound to the Nedd4 C lobe with its C-terminal tail locked in an extended conformation, primed for catalysis. Nedd4-family members are Lys63-specific enzymes whose catalysis is mediated by an essential C-terminal acidic residue |
