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PDBsum entry 2xew

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protein ligands metals Protein-protein interface(s) links
Cell cycle PDB id
2xew

 

 

 

 

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Contents
Protein chain
(+ 6 more) 76 a.a. *
Ligands
EDO ×17
FLC ×2
Metals
_CL ×7
Waters ×651
* Residue conservation analysis
PDB id:
2xew
Name: Cell cycle
Title: Crystal structure of k11-linked diubiquitin
Structure: Ubiquitin. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Engineered: yes. Other_details: ubiquitin polymer linked through lys11 in an isopeptide linkage
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.207     R-free:   0.252
Authors: A.Bremm,S.M.V.Freund,D.Komander
Key ref: A.Bremm et al. (2010). Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nat Struct Biol, 17, 939-947. PubMed id: 20622874
Date:
18-May-10     Release date:   14-Jul-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
685 a.a.
76 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Nat Struct Biol 17:939-947 (2010)
PubMed id: 20622874  
 
 
Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne.
A.Bremm, S.M.Freund, D.Komander.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22157957 J.D.Licchesi, J.Mieszczanek, T.E.Mevissen, T.J.Rutherford, M.Akutsu, S.Virdee, F.El Oualid, J.W.Chin, H.Ovaa, M.Bienz, and D.Komander (2012).
An ankyrin-repeat ubiquitin-binding domain determines TRABID's specificity for atypical ubiquitin chains.
  Nat Struct Mol Biol, 19, 62-71.
PDB code: 3zrh
21118991 A.Hay-Koren, M.Caspi, A.Zilberberg, and R.Rosin-Arbesfeld (2011).
The EDD E3 ubiquitin ligase ubiquitinates and up-regulates beta-catenin.
  Mol Biol Cell, 22, 399-411.  
21540891 C.Behrends, and J.W.Harper (2011).
Constructing and decoding unconventional ubiquitin chains.
  Nat Struct Mol Biol, 18, 520-528.  
21119682 E.W.Harhaj, and V.M.Dixit (2011).
Deubiquitinases in the regulation of NF-κB signaling.
  Cell Res, 21, 22-39.  
  21261459 J.R.McLean, D.Chaix, M.D.Ohi, and K.L.Gould (2011).
State of the APC/C: organization, function, and structure.
  Crit Rev Biochem Mol Biol, 46, 118-136.  
21376237 K.E.Wickliffe, S.Lorenz, D.E.Wemmer, J.Kuriyan, and M.Rape (2011).
The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2.
  Cell, 144, 769-781.  
21266548 M.Akutsu, Y.Ye, S.Virdee, J.W.Chin, and D.Komander (2011).
Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains.
  Proc Natl Acad Sci U S A, 108, 2228-2233.
PDB codes: 3phu 3phw 3phx
21168777 B.A.Malynn, and A.Ma (2010).
Ubiquitin makes its mark on immune regulation.
  Immunity, 33, 843-852.  
  21117055 F.El Oualid, R.Merkx, R.Ekkebus, D.S.Hameed, J.J.Smit, A.de Jong, H.Hilkmann, T.K.Sixma, and H.Ovaa (2010).
Chemical synthesis of ubiquitin, ubiquitin-based probes, and diubiquitin.
  Angew Chem Int Ed Engl, 49, 10149-10153.  
21111228 F.Ikeda, N.Crosetto, and I.Dikic (2010).
What determines the specificity and outcomes of ubiquitin signaling?
  Cell, 143, 677-681.  
21113135 J.N.Dynek, T.Goncharov, E.C.Dueber, A.V.Fedorova, A.Izrael-Tomasevic, L.Phu, E.Helgason, W.J.Fairbrother, K.Deshayes, D.S.Kirkpatrick, and D.Vucic (2010).
c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling.
  EMBO J, 29, 4198-4209.  
20802491 S.Virdee, Y.Ye, D.P.Nguyen, D.Komander, and J.W.Chin (2010).
Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase.
  Nat Chem Biol, 6, 750-757.
PDB code: 2xk5
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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