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PDBsum entry 4br6

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
4br6
Jmol
Contents
Protein chains
196 a.a.
Ligands
GOL
Metals
_NA ×6
MN3 ×4
Waters ×1276
PDB id:
4br6
Name: Oxidoreductase
Title: Crystal structure of chaetomium thermophilum mnsod
Structure: Superoxide dismutase. Chain: a, b, c, d. Synonym: manganese superoxide dismutase. Ec: 1.15.1.1
Source: Chaetomium thermophilum. Organism_taxid: 209285
Resolution:
2.00Å     R-factor:   0.123     R-free:   0.177
Authors: T.Haikarainen,C.Frioux,L.-Q.Zhnag,D.-C.Li,A.C.Papageorgiou
Key ref: T.Haikarainen et al. (2014). Crystal structure and biochemical characterization of a manganese superoxide dismutase from Chaetomium thermophilum. Biochim Biophys Acta, 1844, 422-429. PubMed id: 24316252 DOI: 10.1016/j.bbapap.2013.11.014
Date:
04-Jun-13     Release date:   18-Dec-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
F8V325  (F8V325_9PEZI) -  Superoxide dismutase
Seq:
Struc:
227 a.a.
196 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.15.1.1  - Superoxide dismutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 superoxide + 2 H+ = O2 + H2O2
2 × superoxide
+ 2 × H(+)
= O(2)
+ H(2)O(2)
      Cofactor: Iron or manganese or (zinc and copper)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     superoxide dismutase activity     2 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/j.bbapap.2013.11.014 Biochim Biophys Acta 1844:422-429 (2014)
PubMed id: 24316252  
 
 
Crystal structure and biochemical characterization of a manganese superoxide dismutase from Chaetomium thermophilum.
T.Haikarainen, C.Frioux, L.Q.Zhnag, D.C.Li, A.C.Papageorgiou.
 
  ABSTRACT  
 
A manganese superoxide dismutase from the thermophilic fungus Chaetomium thermophilum (CtMnSOD) was expressed in Pichia pastoris and purified to homogeneity. Its optimal temperature was 60°C with approximately 75% of its activity retained after incubation at 70°C for 60min. Recombinant yeast cells carrying C. thermophilum mnsod gene exhibited higher stress resistance to salt and oxidative stress-inducing agents than control yeast cells. In an effort to provide structural insights, CtMnSOD was crystallized and its structure was determined at 2.0Å resolution. The overall architecture of CtMnSOD was found similar to other MnSODs with highest structural similarities obtained against a MnSOD from the thermotolerant fungus Aspergillus fumigatus. In order to explain its thermostability, structural and sequence analysis of CtMnSOD with other MnSODs was carried out. An increased number of charged residues and an increase in the number of intersubunit salt bridges and the Thr:Ser ratio were identified as potential reasons for the thermostability of CtMnSOD.