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PDBsum entry 2rcv

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protein metals Protein-protein interface(s) links
Oxidoreductase PDB id
2rcv
Jmol
Contents
Protein chains
(+ 2 more) 200 a.a. *
Metals
_MN ×8
Waters ×910
* Residue conservation analysis
PDB id:
2rcv
Name: Oxidoreductase
Title: Crystal structure of the bacillus subtilis superoxide dismutase
Structure: Superoxide dismutase [mn]. Chain: a, b, c, d, e, f, g, h. Synonym: general stress protein 24, gsp24. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: subtilis str. 168. Gene: soda, yqgd. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.60Å     R-factor:   0.211     R-free:   0.230
Authors: P.Liu,H.E.Ewis,Y.J Huang,C.D Lu,P.C Tai,I.T Weber
Key ref: P.Liu et al. (2007). Structure of Bacillus subtilis superoxide dismutase. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 1003-1007. PubMed id: 18084079
Date:
20-Sep-07     Release date:   26-Feb-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P54375  (SODM_BACSU) -  Superoxide dismutase [Mn]
Seq:
Struc:
202 a.a.
200 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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: 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!
  Cellular component     cytoplasm   1 term 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     3 terms  

 

 
    Added reference    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 63:1003-1007 (2007)
PubMed id: 18084079  
 
 
Structure of Bacillus subtilis superoxide dismutase.
P.Liu, H.E.Ewis, Y.J.Huang, C.D.Lu, P.C.Tai, I.T.Weber.
 
  ABSTRACT  
 
The sodA gene of Bacillus subtilis was expressed in Escherichia coli, purified and crystallized. The crystal structure of MnSOD was solved by molecular replacement with four dimers per asymmetric unit and refined to an R factor of 21.1% at 1.8 A resolution. The dimer structure is very similar to that of the related enzyme from B. anthracis. Larger structural differences were observed with the human MnSOD, which has one less helix in the helical domain and a longer loop between two beta-strands and also showed differences in three amino acids at the intersubunit interface in the dimer compared with the two bacterial MnSODs. These structural differences can be exploited in the design of drugs that selectively target the Bacillus enzymes.
 

 

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