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Literature summary for 2.3.2.B8 extracted from

  • Kamadurai, H.B.; Souphron, J.; Scott, D.C.; Duda, D.M.; Miller, D.J.; Stringer, D.; Piper, R.C.; Schulman, B.A.
    Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex (2009), Mol. Cell., 36, 1095-1102.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
determination of the crystal of a complex between the HECT domain NEDD4L and the E2 UbcH5B bearing a covantly-linked ubiquitin at its active site to gain insights of the ubiquitin transfer from an associated E2 to the acceptor cysteine in the HECT domain C-lobe. HECT contains is bilobed, consists of N-terminal N-lobe and C-terminal C-lobe. The C-lobe is essential for the E2-to-E3 ubiquitin transfer and the N-lobe is essential for the the further protein substrate processivity, the transfer of the ubiquitin from E3 to the substrate Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P62837
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Homo sapiens Q96PU5
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Reaction

Reaction Comment Organism Reaction ID
S-ubiquitinyl-[ubiquitin-carrier protein E2]-L-cysteine + [HECT-E3-ubiquitin-carrier protein]-L-cysteine = [ubiquitin-carrier protein E2]-L-cysteine + S-ubiquitinyl-[HECT-E3-ubiquitin-carrier protein]-L-cysteine the 40 kDa C-terminal HET domain binds a reactive thioester-linked E2-ubiquitin covalent-linked complex. The ubiqiutin is transferred from the E2 catalytic cysteine to the HECT domain catalytic cysteine via a transthiolation reaction Homo sapiens

Synonyms

Synonyms Comment Organism
E3 HECT
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Homo sapiens
E3 ubiquitin-protein ligase
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Homo sapiens
UbcH5B-ubiquitin-HECT NEDD4L complex
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Homo sapiens

General Information

General Information Comment Organism
physiological function part of the E1-E2-E3 ubiquitin conjugation cascade. The E2-ubiquitin covalent complex interacts with an E3 (HECT) for ubiquitin transfer. Ubiquitin is transferred to the acceptor cysteine of the C-lobe of the HECT domain Homo sapiens