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PDBsum entry 3e46
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Contents |
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* Residue conservation analysis
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PDB id:
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Ligase
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Title:
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Crystal structure of ubiquitin-conjugating enzyme e2-25kda (huntington interacting protein 2) m172a mutant
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Structure:
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Ubiquitin-conjugating enzyme e2-25 kda. Chain: a. Synonym: ubiquitin-conjugating enzyme e2 k, e2(25k), ubiquitin- protein ligase, ubiquitin carrier protein, huntingtin-interacting protein 2, hip-2. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Organism_taxid: 9606. Gene: ube2k, hip2, lig. Expressed in: escherichia coli.
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Resolution:
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1.86Å
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R-factor:
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0.174
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R-free:
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0.210
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Authors:
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R.C.Hughes,R.C.Wilson,J.W.Flatt,E.J.Meehan,J.D.Ng,P.D.Twigg
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Key ref:
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R.C.Wilson
et al.
(2009).
Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).
Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
440-444.
PubMed id:
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Date:
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09-Aug-08
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Release date:
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26-Aug-08
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PROCHECK
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Headers
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References
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P61086
(UBE2K_HUMAN) -
Ubiquitin-conjugating enzyme E2 K from Homo sapiens
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Seq:
Struc:
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200 a.a.
202 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.2.3.2.23
- E2 ubiquitin-conjugating enzyme.
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Reaction:
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine
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Acta Crystallogr Sect F Struct Biol Cryst Commun
65:440-444
(2009)
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PubMed id:
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Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).
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R.C.Wilson,
R.C.Hughes,
J.W.Flatt,
E.J.Meehan,
J.D.Ng,
P.D.Twigg.
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ABSTRACT
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The ubiquitin-conjugating enzyme E2-25K has been identified as a huntingtin (the
key protein in Huntington's disease) interacting protein and has been shown to
play a role in mediating the toxicity of Abeta, the principal protein involved
in Alzheimer's disease pathogenesis. E2-25K is a dual-domain protein with an
ubiquitin-associated (UBA) domain as well as a conserved ubiquitin-conjugating
(UBC) domain which catalyzes the formation of a covalent bond between the
C-terminal glycine of an ubiquitin molecule and the -amine of a lysine residue
on the acceptor protein as part of the ubiquitin-proteasome pathway. The crystal
structures of E2-25K M172A mutant protein at pH 6.5 and pH 8.5 were determined
to 1.9 and 2.2 A resolution, respectively. Examination of the structures
revealed domain-domain interactions between the UBC and UBA domains which have
not previously been reported.
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Links
