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2.3.2.26: HECT-type E3 ubiquitin transferase

This is an abbreviated version!
For detailed information about HECT-type E3 ubiquitin transferase, go to the full flat file.

Word Map on EC 2.3.2.26

Reaction

[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-lysine
=
[E2 ubiquitin-conjugating enzyme]-L-cysteine
 +
[acceptor protein]-N6-ubiquitinyl-L-lysine

Synonyms

AIP2, AIP4, apoptosis-resistant E3 ligase 1, AREL1, atrophin-1 interacting protein 2, DDB_G0286931, E3 ligase, E3 ubiquitin-protein ligase NEDD4, E3 ubiquitin-protein ligase TOM1, E6-AP, E6AP, ETC-1, HECT domain E3 ubiquitin ligase, HECT ligase, HECT-domain ubiquitin ligase, HECT-type E3 ligase, HECT-type ubiquitin E3 ligase, HECTD3, HectPH1, HECTWWP2, Herc4, Huwe1, Itch, Nedd4, Nedd4 HECT, Nedd4-1, Nedd4L, NEDL1, NleL, RSP5, Smurf1, Smurf2, sog-1, TRIP12, Trp120, UBE3B, Ube3C, ubiquitin-protein ligase E3C, UBR E3 ubiquitin ligase homolog, Ubr-5, UBR1, UBR5, UPL3, UPL5, WW domain-containing E3 Ub–protein ligase 2, WWP1, WWP2

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.26 HECT-type E3 ubiquitin transferase

Crystallization

Crystallization on EC 2.3.2.26 - HECT-type E3 ubiquitin transferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
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
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
hanging drop vapor diffusion method, using 0.1 M HEPES pH 8.4, 0.2 M MgCl2, 15% (v/v) ethanol at 4°C
Huwe1 C-lobe-ubiquitin crystal structure at 2.8 A resolution, by molecular replacement and solution NMR spectroscopy
Smurf2 C-lobe-ubiquitin crystal structure at 2.8 A resolution, by molecular replacement and solution NMR spectroscopy
structure of ubiquitin-loaded human neural precursor cell–expressed 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
structures of Nedd4 HECT domain, alone (2.5 A) and in complex with ubiquitin (2.7 A), showing new binding modes involving two surfaces on ubiquitin and both subdomains of the HECT N-lobes, suggesting an model for the HECT-t-substrate ubiquitin transfer, in which the growing chain on the substrate is kept close to the catalytic cysteine to promote processivity HECTNedd4 displays the typical HECT fold, composed of two lobes connected by a flexible hinge. The N-lobe consists of two moieties, the large and the smal subdomains. The small domains host the E2-binding site and the large carries the catalytic cysteine
structures of ubiquitin variants in complex with the HECT domains of human E3 HECT ligases
-
structures of WWP1 in its fully inactive and partially active states. Domains WW2, L, and WW4 are organized into a headset architecture, in which the WW2 and WW4 domains are bound to bilateral sites within the N-lobe, and L forms a kinked alpha-helix that is tucked into the cleft between the N- and C-lobes of HECT
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