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PDBsum entry 1kkc

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protein metals Protein-protein interface(s) links
Oxidoreductase PDB id
1kkc
Jmol
Contents
Protein chains
200 a.a. *
Metals
_MN ×4
Waters ×745
* Residue conservation analysis
PDB id:
1kkc
Name: Oxidoreductase
Title: Crystal structure of aspergillus fumigatus mnsod
Structure: Manganese superoxide dismutase. Chain: a, b, x, y. Synonym: mnsod. Engineered: yes
Source: Aspergillus fumigatus. Organism_taxid: 5085. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
2.00Å     R-factor:   0.194     R-free:   0.233
Authors: S.Fluckiger,P.R.E.Mittl,L.Scapozza,H.Fijten,G.Folkers, M.G.Grutter,K.Blaser,R.Crameri
Key ref: S.Flückiger et al. (2002). Comparison of the crystal structures of the human manganese superoxide dismutase and the homologous Aspergillus fumigatus allergen at 2-A resolution. J Immunol, 168, 1267-1272. PubMed id: 11801664
Date:
07-Dec-01     Release date:   28-Dec-01    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q92450  (SODM_ASPFU) -  Superoxide dismutase [Mn], mitochondrial
Seq:
Struc:
210 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     intracellular   3 terms 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     5 terms  

 

 
    Added reference    
 
 
J Immunol 168:1267-1272 (2002)
PubMed id: 11801664  
 
 
Comparison of the crystal structures of the human manganese superoxide dismutase and the homologous Aspergillus fumigatus allergen at 2-A resolution.
S.Flückiger, P.R.Mittl, L.Scapozza, H.Fijten, G.Folkers, M.G.Grütter, K.Blaser, R.Crameri.
 
  ABSTRACT  
 
Manganese superoxide dismutase (MnSOD) of Aspergillus fumigatus, a fungus involved in many pulmonary complications, has been identified as IgE-binding protein. It has been shown also that MnSODs from other organisms, including human, are recognized by IgE Abs from individuals sensitized to A. fumigatus MnSOD. Comparison of the fungal and the human crystal structure should allow the identification of structural similarities responsible for IgE-mediated cross-reactivity. The three-dimensional structure of A. fumigatus MnSOD has been determined at 2-A resolution by x-ray diffraction analysis. Crystals belonged to space group P2(1)2(1)2(1) with unit cell dimensions of a = 65.88 A, b = 98.7 A, and c = 139.28 A. The structure was solved by molecular replacement using the structure of the human MnSOD as a search model. The final refined model included four chains of 199-200 amino acids, four manganese ions, and 745 water molecules, with a crystallographic R-factor of 19.4% and a free R-factor of 23.3%. Like MnSODs of other eukaryotic organisms, A. fumigatus MnSOD forms a homotetramer with the manganese ions coordinated by three histidines, one aspartic acid, and one water molecule. The fungal and the human MnSOD share high similarity on the level of both primary and tertiary structure. We identified conserved amino acids that are solvent exposed in the fungal and the human crystal structure and are therefore potentially involved in IgE-mediated cross-reactivity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20972560 H.Xiang, G.Pan, C.R.Vossbrinck, R.Zhang, J.Xu, T.Li, Z.Zhou, C.Lu, and Z.Xiang (2010).
A tandem duplication of manganese superoxide dismutase in Nosema bombycis and its evolutionary origins.
  J Mol Evol, 71, 401-414.  
  19052361 C.H.Trinh, T.Hunter, E.E.Stewart, S.E.Phillips, and G.J.Hunter (2008).
Purification, crystallization and X-ray structures of the two manganese superoxide dismutases from Caenorhabditis elegans.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1110-1114.
PDB codes: 3dc5 3dc6
17029625 P.Bowyer, M.Fraczek, and D.W.Denning (2006).
Comparative genomics of fungal allergens and epitopes shows widespread distribution of closely related allergen and epitope orthologues.
  BMC Genomics, 7, 251.  
16055318 E.Fréalle, C.Noël, E.Viscogliosi, D.Camus, E.Dei-Cas, and L.Delhaes (2005).
Manganese superoxide dismutase in pathogenic fungi: an issue with pathophysiological and phylogenetic involvements.
  FEMS Immunol Med Microbiol, 45, 411-422.  
15128298 A.Andersson, O.Rasool, M.Schmidt, R.Kodzius, S.Flückiger, A.Zargari, R.Crameri, and A.Scheynius (2004).
Cloning, expression and characterization of two new IgE-binding proteins from the yeast Malassezia sympodialis with sequence similarities to heat shock proteins and manganese superoxide dismutase.
  Eur J Biochem, 271, 1885-1894.  
14686801 A.Vojdani, A.Kashanian, E.Vojdani, and A.W.Campbell (2003).
Saliva secretory IgA antibodies against molds and mycotoxins in patients exposed to toxigenic fungi.
  Immunopharmacol Immunotoxicol, 25, 595-614.  
12906780 V.P.Kurup (2003).
Fungal allergens.
  Curr Allergy Asthma Rep, 3, 416-423.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.