4BBN

NEDD4 HECT-Ub:Ub complex

Summary for 4BBN

• Entry DOI: 10.2210/pdb4bbn/pdb
• Related: 2XBB 2XBF 4BE8
• Descriptor: E3 UBIQUITIN-PROTEIN LIGASE NEDD4, POLYUBIQUITIN-B, ... (4 entities in total)
• Functional Keywords: ligase-signaling protein complex, ligase, ubiquitination, ligase/signaling protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm (By similarity): P46934 P0CG53 P0CG53
• Total number of polymer chains: 3
• Total formula weight: 62830.66

Authors

Maspero, E.,Valentini, E.,Mari, S.,Cecatiello, V.,Polo, S.,Pasqualato, S. (deposition date: 2012-09-27, release date: 2013-05-01, Last modification date: 2023-12-20)

Primary citation

Maspero, E.,Valentini, E.,Mari, S.,Cecatiello, V.,Soffientini, P.,Pasqualato, S.,Polo, S.
Structure of a Ubiquitin-Loaded Hect Ligase Reveals the Molecular Basis for Catalytic Priming
Nat.Struct.Mol.Biol., 20:696-, 2013

PubMed Abstract: Homologous to E6-AP C terminus (HECT) E3 ligases recognize and directly catalyze ligation of ubiquitin (Ub) to their substrates. Molecular details of this process remain unknown. We report the first structure, to our knowledge, of a Ub-loaded E3, the human neural precursor cell-expressed developmentally downregulated protein 4 (Nedd4). The HECT(Nedd4)~Ub transitory intermediate provides a structural basis for the proposed sequential addition mechanism. The donor Ub, transferred from the E2, is bound to the Nedd4 C lobe with its C-terminal tail locked in an extended conformation, primed for catalysis. We provide evidence that the Nedd4-family members are Lys63-specific enzymes whose catalysis is mediated by an essential C-terminal acidic residue.

PubMed: 23644597
DOI: 10.1038/NSMB.2566

Experimental method

X-RAY DIFFRACTION (2.51 Å)