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PDBsum entry 1gv3

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protein metals Protein-protein interface(s) links
Manganese superoxide dismutase PDB id
1gv3
Jmol
Contents
Protein chains
214 a.a. *
Metals
_MN ×2
Waters ×166
* Residue conservation analysis
PDB id:
1gv3
Name: Manganese superoxide dismutase
Title: The 2.0 angstrom resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase
Structure: Manganese superoxide dismutase. Chain: a, b. Fragment: helical hairpin, alpha/beta domain, residues 30-270. Engineered: yes
Source: Anabaena sp.. Organism_taxid: 103690. Strain: pcc 7120. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
Resolution:
2.00Å     R-factor:   0.188     R-free:   0.211
Authors: W.Atzenhofer,G.Regelsberger,U.Jacob,R.Huber,G.A.Peschek, C.Obinger
Key ref:
W.Atzenhofer et al. (2002). The 2.0A resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase. J Mol Biol, 321, 479-489. PubMed id: 12162960 DOI: 10.1016/S0022-2836(02)00624-1
Date:
05-Feb-02     Release date:   08-Aug-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8Z0M1  (Q8Z0M1_NOSS1) -  Superoxide dismutase
Seq:
Struc:
270 a.a.
214 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     superoxide dismutase activity     2 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/S0022-2836(02)00624-1 J Mol Biol 321:479-489 (2002)
PubMed id: 12162960  
 
 
The 2.0A resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase.
W.Atzenhofer, G.Regelsberger, U.Jacob, G.Peschek, P.Furtmüller, R.Huber, C.Obinger.
 
  ABSTRACT  
 
Cyanobacteria are shown to be unique in containing membrane-bound manganese superoxide dismutases (MnSOD). They are homodimeric type 2 membrane proteins that protect this phototrophic organism against oxidative stress. We have determined, for the first time, the 2.0A resolution structure of the catalytic portion of the MnSOD from the filamentous cyanobacterium Anabaena PCC 7120. Within each subunit, both the N-terminal helical hairpin (His94 and His145) and the C-terminal alpha/beta domain (His232 and Asp228) contribute ligands to the catalytic manganese site. Together with a water or hydroxide ion (OH(x)) a five-coordinated trigonal bipyramidal geometry is formed, with OH(x) and His90 forming the axial ligands and manganese shifted out of the equatorial plane in the direction of OH(x). The ligands including OH(x) are tightly constrained by hydrogen bonding with surrounding residues either from the same monomer (Tyr98, Asn144, Trp194, Gln213, Val229, Trp230) or from the neighbouring subunit (Glu231, Tyr235). This underlines the important role of the symmetric dimeric structure of MnSODs in contributing elements to both the active site and the substrate funnel. The Mn cdots, three dots, centered Mn distance (18.4A) is bridged by the hydrogen-bonded His232 of one monomer with Glu231 of the other monomer. A detailed discussion of the structure, a comparison with known structures of soluble MnSODs as well as a model of the cyanobacterial membrane-bound MnSOD is presented.
 
  Selected figure(s)  
 
Figure 6.
Figure 6. Overlay of tube representations of T. thermophilus (blue) and Anabaena PCC 7120 MnSOD dimers (red). The manganese ion is drawn as a yellow sphere. Figure 6, Figure 7 and Figure 8 were produced using MOLSCRIPT. [39 and 40]
Figure 8.
Figure 8. Diagram of the symmetric dimer interface. Residues from each subunit are shown in either orange or yellow. Ribbons are rendered in light blue or brown. Direct interactions between amino acid residues of opposing chains are shown as broken green lines labeled by the corresponding bond length in Å.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 321, 479-489) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20525290 B.Priya, R.K.Sivaprasanth, V.D.Jensi, L.Uma, G.Subramanian, and D.Prabaharan (2010).
Characterization of manganese superoxide dismutase from a marine cyanobacterium Leptolyngbya valderiana BDU20041.
  Saline Systems, 6, 6.  
  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
18042279 B.Priya, J.Premanandh, R.T.Dhanalakshmi, T.Seethalakshmi, L.Uma, D.Prabaharan, and G.Subramanian (2007).
Comparative analysis of cyanobacterial superoxide dismutases to discriminate canonical forms.
  BMC Genomics, 8, 435.  
17983264 C.H.Yeang, and D.Haussler (2007).
Detecting coevolution in and among protein domains.
  PLoS Comput Biol, 3, e211.  
17307750 W.Zhao, Q.Guo, and J.Zhao (2007).
A membrane-associated Mn-superoxide dismutase protects the photosynthetic apparatus and nitrogenase from oxidative damage in the Cyanobacterium Anabaena sp. PCC 7120.
  Plant Cell Physiol, 48, 563-572.  
15032833 G.A.Peschek, C.Obinger, and M.Paumann (2004).
The respiratory chain of blue-green algae (cyanobacteria).
  Physiol Plant, 120, 358-369.  
15302891 G.Regelsberger, U.Laaha, D.Dietmann, F.Rüker, A.Canini, M.Grilli-Caiola, P.G.Furtmüller, C.Jakopitsch, G.A.Peschek, and C.Obinger (2004).
The iron superoxide dismutase from the filamentous cyanobacterium Nostoc PCC 7120. Localization, overexpression, and biochemical characterization.
  J Biol Chem, 279, 44384-44393.  
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.