PDBsum entry 2z6o

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protein metals links
Ligase PDB id
Protein chain
166 a.a. *
Waters ×127
* Residue conservation analysis
PDB id:
Name: Ligase
Title: Crystal structure of the ufc1, ufm1 conjugating enzyme 1
Structure: Ufm1-conjugating enzyme 1. Chain: a. Synonym: ubiquitin-fold modifier-conjugating enzyme 1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ufc1. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.60Å     R-factor:   0.196     R-free:   0.221
Authors: T.Mizushima,K.Tatsumi,Y.Ozaki,T.Kawakami,A.Suzuki, K.Ogasahara,M.Komatsu,E.Kominami,K.Tanaka,T.Yamane
Key ref: T.Mizushima et al. (2007). Crystal structure of Ufc1, the Ufm1-conjugating enzyme. Biochem Biophys Res Commun, 362, 1079-1084. PubMed id: 17825256 DOI: 10.1016/j.bbrc.2007.08.129
06-Aug-07     Release date:   25-Sep-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9Y3C8  (UFC1_HUMAN) -  Ubiquitin-fold modifier-conjugating enzyme 1
167 a.a.
166 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular vesicular exosome   1 term 
  Biological process     protein ufmylation   2 terms 
  Biochemical function     UFM1 conjugating enzyme activity     2 terms  


DOI no: 10.1016/j.bbrc.2007.08.129 Biochem Biophys Res Commun 362:1079-1084 (2007)
PubMed id: 17825256  
Crystal structure of Ufc1, the Ufm1-conjugating enzyme.
T.Mizushima, K.Tatsumi, Y.Ozaki, T.Kawakami, A.Suzuki, K.Ogasahara, M.Komatsu, E.Kominami, K.Tanaka, T.Yamane.
Ubiquitin and ubiquitin-like protein-conjugating enzymes play central roles in posttranslational modification processes. The ubiquitin-fold modifier 1 (Ufm1), one of a variety of ubiquitin-like modifiers, is covalently attached to target proteins via Uba5 and Ufm1-conjugating enzyme 1 (Ufc1), which are analogous to the E1 and E2 ubiquitylation enzymes. As Ufm1-related proteins are conserved in metazoa and plants, the Ufm1 system likely plays important roles in various multicellular organisms. Herein, we report the X-ray structure of human Ufc1 determined at 1.6 A resolution. The Ufc1 structure comprises a canonical E2 domain and an additional N-terminal domain. The Uba5 binding site on Ufc1 was assigned by structural comparison of Ufc1 and Ubc12 and related mutational analyses. In addition, we show that the N-terminal unique domain of Ufc1 contributes to thermal stability.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20018847 K.Tatsumi, Y.S.Sou, N.Tada, E.Nakamura, S.Iemura, T.Natsume, S.H.Kang, C.H.Chung, M.Kasahara, E.Kominami, M.Yamamoto, K.Tanaka, and M.Komatsu (2010).
A novel type of E3 ligase for the Ufm1 conjugation system.
  J Biol Chem, 285, 5417-5427.  
19352404 B.A.Schulman, and J.W.Harper (2009).
Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways.
  Nat Rev Mol Cell Biol, 10, 319-331.  
19101823 G.Liu, F.Forouhar, A.Eletsky, H.S.Atreya, J.M.Aramini, R.Xiao, Y.J.Huang, M.Abashidze, J.Seetharaman, J.Liu, B.Rost, T.Acton, G.T.Montelione, J.F.Hunt, and T.Szyperski (2009).
NMR and X-RAY structures of human E2-like ubiquitin-fold modifier conjugating enzyme 1 (UFC1) reveal structural and functional conservation in the metazoan UFM1-UBA5-UFC1 ubiquination pathway.
  J Struct Funct Genomics, 10, 127-136.
PDB codes: 2k07 3e2g 3evx
18276160 A.M.Burroughs, M.Jaffee, L.M.Iyer, and L.Aravind (2008).
Anatomy of the E2 ligase fold: implications for enzymology and evolution of ubiquitin/Ub-like protein conjugation.
  J Struct Biol, 162, 205-218.  
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