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PDBsum entry 3h1u

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protein metals Protein-protein interface(s) links
Signaling protein PDB id
3h1u

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
75 a.a. *
Metals
_CD ×5
Waters ×42
* Residue conservation analysis
PDB id:
3h1u
Name: Signaling protein
Title: Structure of ubiquitin in complex with cd ions
Structure: Ubiquitin. Chain: a, b
Source: Bos taurus. Bovine. Organism_taxid: 9913
Resolution:
3.00Å     R-factor:   0.222     R-free:   0.257
Authors: I.A.Qureshi,F.Ferron,P.Cheung,J.Lescar
Key ref: I.A.Qureshi et al. (2009). Crystallographic structure of ubiquitin in complex with cadmium ions. Bmc Res Notes, 2, 251. PubMed id: 20003470
Date:
14-Apr-09     Release date:   05-May-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0CH28  (UBC_BOVIN) -  Polyubiquitin-C from Bos taurus
Seq:
Struc:
 
Seq:
Struc:
690 a.a.
75 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

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

 

 
Bmc Res Notes 2:251 (2009)
PubMed id: 20003470  
 
 
Crystallographic structure of ubiquitin in complex with cadmium ions.
I.A.Qureshi, F.Ferron, C.C.Seh, P.Cheung, J.Lescar.
 
  ABSTRACT  
 
BACKGROUND: Ubiquitination plays a critical role in regulating many cellular processes, from DNA repair and gene transcription to cell cycle and apoptosis. It is catalyzed by a specific enzymatic cascade ultimately leading to the conjugation of ubiquitin to lysine residues of the target protein that can be the ubiquitin molecule itself and to the formation of poly-ubiquitin chains. FINDINGS: We present the crystal structure at 3.0 A resolution of bovine ubiquitin crystallized in presence of cadmium ions. Two molecules of ubiquitin are present in the asymmetric unit. Interestingly this non-covalent dimeric arrangement brings Lys-6 and Lys-63 of each crystallographically-independent monomer in close contact with the C-terminal ends of the other monomer. Residues Leu-8, Ile-44 and Val-70 that form a hydrophobic patch at the surface of the Ub monomer are trapped at the dimer interface. CONCLUSIONS: The structural basis for signalling by poly-Ub chains relies on a visualization of conformations of alternatively linked poly-Ub chains. This arrangement of ubiquitin could illustrate how linkages involving Lys-6 or Lys-63 of ubiquitin are produced in the cell. It also details how ubiquitin molecules can specifically chelate cadmium ions.
 

 

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