PDBsum entry 1wb7

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Oxidoreductase PDB id
Protein chains
205 a.a. *
_FE ×2
Waters ×224
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Iron superoxide dismutase (fe-sod) from the hyperthermophile sulfolobus solfataricus. Crystal structure of the y41f mutant.
Structure: Superoxide dismutase [fe]. Chain: a, b. Engineered: yes. Mutation: yes
Source: Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PDB file)
2.24Å     R-factor:   0.181     R-free:   0.209
Authors: M.A.Gogliettino,F.Tanfani,A.Scire,T.Ursby,B.S.Adinolfi, T.Cacciamani,E.De Vendittis
Key ref:
M.A.Gogliettino et al. (2004). The role of Tyr41 and His155 in the functional properties of superoxide dismutase from the archaeon Sulfolobus solfataricus. Biochemistry, 43, 2199-2208. PubMed id: 14979716 DOI: 10.1021/bi035661y
31-Oct-04     Release date:   08-Nov-04    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P80857  (SODF_SULSO) -  Superoxide dismutase [Fe]
211 a.a.
205 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.  - 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    
DOI no: 10.1021/bi035661y Biochemistry 43:2199-2208 (2004)
PubMed id: 14979716  
The role of Tyr41 and His155 in the functional properties of superoxide dismutase from the archaeon Sulfolobus solfataricus.
M.A.Gogliettino, F.Tanfani, A.Sciré, T.Ursby, B.S.Adinolfi, T.Cacciamani, E.De Vendittis.
We have examined and compared the effects of mutating Y41 and H155 in the iron superoxide dismutase (SOD) from the archaeon Sulfolobus solfataricus (Ss). These two neighboring residues in the active site are known to have crucial functions in structurally related SODs from different sources. The metal analysis indicates a slightly lower iron content after either Y41F or H155Q replacement, without any significant substitution of iron for manganese. The specific activity of SsSOD referred to the iron content is 17-fold reduced in the Y41F mutant, whereas it is less than 2-fold reduced by the H155Q mutation. The noticeable pH dependence of the activity of SsSOD and H155Q-SsSOD, due to the ionization of Y41 (pK 8.4), is lost in Y41F-SsSOD. After H155Q and even more after the Y41F substitution, the archaeal enzyme acquires a moderate sensitivity to sodium azide inhibition. The hydrogen peroxide inactivation of SsSOD is significantly increased after H155Q replacement; however, both mutants are insensitive to the modification of residue 41 by phenylmethanesulfonyl fluoride. Heat inactivation studies showed that the high stability of SsSOD is reduced by the H155Q mutation; however, upon the addition of SDS, a much faster inactivation kinetics is observed both with wild-type and mutant SsSOD forms. The detergent is also required to follow thermal denaturation of the archaeal enzyme by Fourier transform infrared spectroscopy; these studies gave information about the effect of mutations and modification on flexibility and compactness of the protein structure. The crystal structure of Y41F mutant revealed an uninterrupted hydrogen bond network including three solvent molecules connecting the iron-ligating hydroxide ion via H155 with F41 and H37, which is not present in structures of the corresponding mutant SODs from other sources. These data suggest that Y41 and H155 are important for the structural and functional properties of SsSOD; in particular, Y41 seems to be a powerful regulator of the activity of SsSOD, whereas H155 is apparently involved in the organization of the active site of the enzyme.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19384983 I.Castellano, F.Cecere, A.De Vendittis, R.Cotugno, A.Chambery, A.Di Maro, A.Michniewicz, G.Parlato, M.Masullo, E.V.Avvedimento, E.De Vendittis, and M.R.Ruocco (2009).
Rat mitochondrial manganese superoxide dismutase: Amino acid positions involved in covalent modifications, activity, and heat stability.
  Biopolymers, 91, 1215-1226.  
18506781 A.Scirè, A.Marabotti, V.Aurilia, M.Staiano, P.Ringhieri, L.Iozzino, R.Crescenzo, F.Tanfani, and S.D'Auria (2008).
Molecular strategies for protein stabilization: the case of a trehalose/maltose-binding protein from Thermus thermophilus.
  Proteins, 73, 839-850.  
17912757 R.Wintjens, D.Gilis, and M.Rooman (2008).
Mn/Fe superoxide dismutase interaction fingerprints and prediction of oligomerization and metal cofactor from sequence.
  Proteins, 70, 1564-1577.  
16381845 C.P.Toseland, H.McSparron, M.N.Davies, and D.R.Flower (2006).
PPD v1.0--an integrated, web-accessible database of experimentally determined protein pKa values.
  Nucleic Acids Res, 34, D199-D203.  
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