PDBsum entry 3ce1

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Oxidoreductase PDB id
Protein chain
150 a.a. *
Waters ×154
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Crystal structure of the cu/zn superoxide dismutase from cryptococcus liquefaciens strain n6
Structure: Superoxide dismutase [cu-zn]. Chain: a. Synonym: cu/zn superoxide dismutase. Engineered: yes
Source: Cryptococcus liquefaciens. Organism_taxid: 104408. Strain: n6. Gene: c-sod1. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.20Å     R-factor:   0.150     R-free:   0.166
Authors: A.H.Teh,S.Kanamasa,S.Kajiwara,T.Kumasaka
Key ref: A.H.Teh et al. (2008). Structure of Cu/Zn superoxide dismutase from the heavy-metal-tolerant yeast Cryptococcus liquefaciens strain N6. Biochem Biophys Res Commun, 374, 475-478. PubMed id: 18640099 DOI: 10.1016/j.bbrc.2008.07.046
27-Feb-08     Release date:   26-Aug-08    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
A0ZPR9  (A0ZPR9_9TREE) -  Superoxide dismutase [Cu-Zn]
157 a.a.
150 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Superoxide dismutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 superoxide + 2 H+ = O2 + H2O2
2 × superoxide
+ 2 × H(+)
= O(2)
+ H(2)O(2)
      Cofactor: Fe cation or Mn(2+) or (Zn(2+) and Cu cation)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     3 terms  


    Added reference    
DOI no: 10.1016/j.bbrc.2008.07.046 Biochem Biophys Res Commun 374:475-478 (2008)
PubMed id: 18640099  
Structure of Cu/Zn superoxide dismutase from the heavy-metal-tolerant yeast Cryptococcus liquefaciens strain N6.
A.H.Teh, S.Kanamasa, S.Kajiwara, T.Kumasaka.
The deep-sea yeast Cryptococcus liquefaciens strain N6 shows high tolerance towards heavy metals, and can grow in the presence of high concentrations of copper ions. Enzymatic analysis indicated that copper ions induced the Cu/Zn superoxide dismutase activity of strain N6 (Cl-SOD1). In this study, the 1.2A resolution crystal structure of Cl-SOD1 has revealed several significant residue substitutions compared to the other Cu/Zn SODs. In the electrostatic loop, notably, His135 and Pro136 replace the well-conserved linear residues, while Thr133 substitutes a highly conserved glycine. The electrostatic loop has been shown to be involved in the copper uptake process, and these substitutions have caused an inward dragging of the turn region of the loop. As the introduction of proline and abolishment of glycine decrease loop flexibility, this structural reorganization may have helped stabilize the loop conformation, possibly resulting in more efficient copper uptake and a more stabilized copper-bound form.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20516618 I.Ascone, C.Savino, R.Kahn, and R.Fourme (2010).
Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa.
  Acta Crystallogr D Biol Crystallogr, 66, 654-663.
PDB code: 3hw7
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