 |
PDBsum entry 4be8
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Structure of a ubiquitin-Loaded hect ligase reveals the molecular basis for catalytic priming.
|
|
|
Authors
|
|
E.Maspero,
E.Valentini,
S.Mari,
V.Cecatiello,
P.Soffientini,
S.Pasqualato,
S.Polo.
|
|
|
Ref.
|
|
Nat Struct Biol, 2013,
20,
696-701.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
