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PDBsum entry 3f92

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protein ligands metals links
Ligase PDB id
3f92
Jmol
Contents
Protein chain
202 a.a. *
Ligands
PG4 ×2
BME
TRS
Metals
_CA
Waters ×89
* Residue conservation analysis
PDB id:
3f92
Name: Ligase
Title: Crystal structure of ubiquitin-conjugating enzyme e2-25kda (huntington interacting protein 2) m172a mutant crystallized at ph 8.5
Structure: Ubiquitin-conjugating enzyme e2 k, chimera with azorectase. Chain: a. Synonym: ubiquitin-conjugating enzyme e2-25 kda, e2(25k), ubiquitin-protein ligase, ubiquitin carrier protein, huntington-interacting protein 2, hip-2. Engineered: yes. Mutation: yes
Source: Homo sapiens. Organism_taxid: 9606. Gene: ube2k, hip2, lig. Expressed in: escherichia coli.
Resolution:
2.23Å     R-factor:   0.174     R-free:   0.213
Authors: R.C.Wilson,R.C.Hughes,J.W.Flatt,E.J.Meehan,J.D.Ng,P.D.Twigg
Key ref: 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: 19407372
Date:
13-Nov-08     Release date:   25-Nov-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P61086  (UBE2K_HUMAN) -  Ubiquitin-conjugating enzyme E2 K
Seq:
Struc:
200 a.a.
202 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.6.3.2.19  - Ubiquitin--protein ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine
ATP
+ ubiquitin
+ protein lysine
= AMP
+ diphosphate
+ protein N-ubiquityllysine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     protein K48-linked ubiquitination   5 terms 
  Biochemical function     nucleotide binding     8 terms  

 

 
    reference    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 65:440-444 (2009)
PubMed id: 19407372  
 
 
Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).
R.C.Wilson, R.C.Hughes, J.W.Flatt, E.J.Meehan, J.D.Ng, P.D.Twigg.
 
  ABSTRACT  
 
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.