PDBsum entry 2bpi

Oxidoreductase

PDB id: 2bpi

Contents

Protein chains

197 a.a. *

Metals

_FE ×2

Waters ×140

* Residue conservation analysis

PDB id:

2bpi

Name:

Oxidoreductase

Title:

Structure of iron dependent superoxide dismutase from p. Falciparum.

Structure:

Fe-superoxide dismutase. Chain: a, b. Engineered: yes

Source:

Plasmodium falciparum. Organism_taxid: 36329. Strain: 3d7. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

2.52Å R-factor: 0.187 R-free: 0.263

Authors:

I.W.Boucher,J.Brannigan,A.J.Wilkinson,M.Brzozowski

Key ref:

I.W.Boucher et al. (2006). The crystal structure of superoxide dismutase from Plasmodium falciparum. Bmc Struct Biol, 6, 20. PubMed id: 17020617

Date:

20-Apr-05 Release date: 11-Oct-06

Protein chains

Q8IAY6  (SODF_PLAF7) -  Superoxide dismutase [Fe] from Plasmodium falciparum (isolate 3D7)

Seq: 198 a.a.

Struc: 197 a.a.

Enzyme reactions

• Enzyme class: E.C.1.15.1.1 - superoxide dismutase.
• Reaction: 2 superoxide + 2 H⁺ = H2O2 + O2
• Cofactor: Fe cation or Mn(2+) or (Zn(2+) and Cu cation)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

Bmc Struct Biol 6:20 (2006)

PubMed id: 17020617

The crystal structure of superoxide dismutase from Plasmodium falciparum.

I.W.Boucher, A.M.Brzozowski, J.A.Brannigan, C.Schnick, D.J.Smith, S.A.Kyes, A.J.Wilkinson.

ABSTRACT

BACKGROUND: Superoxide dismutases (SODs) are important enzymes in defence against oxidative stress. In Plasmodium falciparum, they may be expected to have special significance since part of the parasite life cycle is spent in red blood cells where the formation of reactive oxygen species is likely to be promoted by the products of haemoglobin breakdown. Thus, inhibitors of P. falciparum SODs have potential as anti-malarial compounds. As a step towards their development we have determined the crystal structure of the parasite's cytosolic iron superoxide dismutase. RESULTS: The cytosolic iron superoxide dismutase from P. falciparum (PfFeSOD) has been overexpressed in E. coli in a catalytically active form. Its crystal structure has been solved by molecular replacement and refined against data extending to 2.5 A resolution. The structure reveals a two-domain organisation and an iron centre in which the metal is coordinated by three histidines, an aspartate and a solvent molecule. Consistent with ultracentrifugation analysis the enzyme is a dimer in which a hydrogen bonding lattice links the two active centres. CONCLUSION: The tertiary structure of PfFeSOD is very similar to those of a number of other iron-and manganese-dependent superoxide dismutases, moreover the active site residues are conserved suggesting a common mechanism of action. Comparison of the dimer interfaces of PfFeSOD with the human manganese-dependent superoxide dismutase reveals a number of differences, which may underpin the design of parasite-selective superoxide dismutase inhibitors.