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PDBsum entry 2cw2

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protein metals Protein-protein interface(s) links
Oxidoreductase PDB id
2cw2
Jmol
Contents
Protein chains
199 a.a. *
Metals
_FE ×2
Waters ×409
* Residue conservation analysis
PDB id:
2cw2
Name: Oxidoreductase
Title: Crystal structure of superoxide dismutase from p. Marinus
Structure: Superoxide dismutase 1. Chain: a, b. Engineered: yes
Source: Perkinsus marinus. Organism_taxid: 31276. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.86Å     R-factor:   0.173     R-free:   0.216
Authors: O.A.Asojo,E.J.Schott,G.R.Vasta,A.M.Silva
Key ref:
O.A.Asojo et al. (2006). Structures of PmSOD1 and PmSOD2, two superoxide dismutases from the protozoan parasite Perkinsus marinus. Acta Crystallograph Sect F Struct Biol Cryst Commun, 62, 1072-1075. PubMed id: 17077482 DOI: 10.1107/S1744309106040425
Date:
16-Jun-05     Release date:   04-Jul-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8ISJ0  (Q8ISJ0_9ALVE) -  Superoxide dismutase
Seq:
Struc:
226 a.a.
199 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   3 terms 
  Biochemical function     oxidoreductase activity     3 terms  

 

 
    Added reference    
 
 
DOI no: 10.1107/S1744309106040425 Acta Crystallograph Sect F Struct Biol Cryst Commun 62:1072-1075 (2006)
PubMed id: 17077482  
 
 
Structures of PmSOD1 and PmSOD2, two superoxide dismutases from the protozoan parasite Perkinsus marinus.
O.A.Asojo, E.J.Schott, G.R.Vasta, A.M.Silva.
 
  ABSTRACT  
 
Perkinsus marinus, a facultative intracellular parasite of the eastern oyster Crassostrea virginica, is responsible for mass mortalities of oyster populations. P. marinus trophozoites survive and proliferate within oyster hemocytes, invading most tissues and fluids, thus causing a systemic infection that eventually kills the host. The phagocytosis of P. marinus trophozoites lacks a respiratory burst, suggesting that the parasite has mechanisms that actively abrogate the host's oxidative defense responses. One mechanism and the first line of defense against oxidative damage is the dismutation of superoxide radical to molecular oxygen and hydrogen peroxide by superoxide dismutases (SODs). P. marinus possesses two iron-cofactored SODs, PmSOD1 and PmSOD2. Here, the crystallization and X-ray structures of both PmSOD1 and PmSOD2 are presented.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 (a) Ribbon diagram of the PmSOD1 dimer showing Fe ions (purple spheres) at the active sites with their ligands. At the center of the figure, Glu165 interacts across the dimer interface with the metal ligand His166. (b) Close-up of the active site of PmSOD1 shows the Fe ion (represented as a large yellow sphere) coordinated by three histidine residues, an aspartic acid residue and a water molecule. The water molecule, whose O-atom location is represented as a small red sphere, is coordinated by Gln76.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 1072-1075) copyright 2006.  
  Figure was selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20374649 S.J.Joseph, J.A.Fernández-Robledo, M.J.Gardner, N.M.El-Sayed, C.H.Kuo, E.J.Schott, H.Wang, J.C.Kissinger, and G.R.Vasta (2010).
The Alveolate Perkinsus marinus: biological insights from EST gene discovery.
  BMC Genomics, 11, 228.  
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