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PDBsum entry 4be8
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PDB id:
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Ligase
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Title:
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Nedd4 hect a889f structure
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Structure:
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E3 ubiquitin-protein ligase nedd4. Chain: a. Fragment: hect domain, residues 519-900. Synonym: cell proliferation-inducing gene 53 protein, neural precursor cell expressed developmentally down-regulated protein 4, nedd-4. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.
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Resolution:
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3.00Å
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R-factor:
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0.248
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R-free:
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0.295
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Authors:
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E.Maspero,E.Valentini,S.Mari,V.Cecatiello,S.Polo,S.Pasqualato
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Key ref:
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E.Maspero
et al.
(2013).
Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming.
Nat Struct Biol,
20,
696-701.
PubMed id:
DOI:
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Date:
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06-Mar-13
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Release date:
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01-May-13
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PROCHECK
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Headers
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References
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P46934
(NEDD4_HUMAN) -
E3 ubiquitin-protein ligase NEDD4 from Homo sapiens
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Seq:
Struc:
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1319 a.a.
378 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 6 residue positions (black
crosses)
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Enzyme class:
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E.C.2.3.2.26
- HECT-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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DOI no:
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Nat Struct Biol
20:696-701
(2013)
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PubMed id:
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Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming.
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E.Maspero,
E.Valentini,
S.Mari,
V.Cecatiello,
P.Soffientini,
S.Pasqualato,
S.Polo.
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ABSTRACT
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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.
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Links
