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3JVZ

E2~Ubiquitin-HECT

Summary for 3JVZ
Entry DOI10.2210/pdb3jvz/pdb
Related3JW0
DescriptorUbiquitin-conjugating enzyme E2 D2, E3 ubiquitin-protein ligase NEDD4-like, Ubiquitin (3 entities in total)
Functional Keywordsubiquitin, hect, e3, ubiquitin ligase, ubch5b, nedd4l, nedd4-2, ligase, ubl conjugation pathway, host-virus interaction, ligase-signaling protein complex, ligase/signaling protein
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm: Q96PU5
Total number of polymer chains6
Total formula weight141935.48
Authors
Souphron, J.,Kamadurai, H.B.,Schulman, B.A. (deposition date: 2009-09-17, release date: 2010-01-12, Last modification date: 2024-10-09)
Primary citationKamadurai, 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.
Mol.Cell, 36:1095-1102, 2009
Cited by
PubMed Abstract: In E1-E2-E3 ubiquitin (Ub) conjugation cascades, the E2 first forms a transient E2 approximately Ub covalent complex and then interacts with an E3 for Ub transfer. For cascades involving E3s in the HECT class, Ub is transferred from an associated E2 to the acceptor cysteine in the HECT domain C lobe. To gain insights into this process, we determined the crystal structure of a complex between the HECT domain of NEDD4L and the E2 UbcH5B bearing a covalently linked Ub at its active site (UbcH5B approximately Ub). Noncovalent interactions between UbcH5B and the HECT N lobe and between Ub and the HECT domain C lobe lead to an overall compact structure, with the Ub C terminus sandwiched between UbcH5B and HECT domain active sites. The structure suggests a model for E2-to-HECT Ub transfer, in which interactions between a donor Ub and an acceptor domain constrain upstream and downstream enzymes for conjugation.
PubMed: 20064473
DOI: 10.1016/j.molcel.2009.11.010
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.3 Å)
Structure validation

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