ArticleBMC structural biology2006
The crystal structure of superoxide dismutase from Plasmodium falciparum.
Article in BMC structural biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
- Superoxide Dismutases in Immune Regulation and Infectious Diseases.Antioxidants (Basel, Switzerland) · 2025Review
- Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress.Scientific reports · 2019Article
- Crystal structure of an iron superoxide dismutase from the pathogenic amoeba Acanthamoeba castellanii.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Identification of new promising Plasmodium falciparum superoxide dismutase allosteric inhibitors through hierarchical pharmacophore-based virtual screening and molecular dynamics.Journal of molecular modeling · 2018Article
- Chemical Warfare at the Microorganismal Level: A Closer Look at the Superoxide Dismutase Enzymes of Pathogens.ACS infectious diseases · 2018Review
- Extensive gain and loss of photosystem I subunits in chromerid algae, photosynthetic relatives of apicomplexans.Scientific reports · 2017Article
- The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.Molecules (Basel, Switzerland) · 2016Review
- Iron superoxide dismutases in eukaryotic pathogens: new insights from Apicomplexa and Trypanosoma structures.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma cruzi iron-superoxide dismutases (Fe-SODs) A and B: disparate susceptibilities due to the repair of Tyr35 radical by Cys83 in Fe-SODB through intramolecular electron transfer.The Journal of biological chemistry · 2014Article
- Dual-functioning antimalarials that inhibit the chloroquine-resistance transporter.Future microbiology · 2013Review
- Functional expression and characterization of an iron-containing superoxide dismutase of Acanthamoeba castellanii.Parasitology research · 2012Article
- The crystal structures of macrophage migration inhibitory factor from Plasmodium falciparum and Plasmodium berghei.Protein science : a publication of the Protein Society · 2009Article
- Identification and characterization of a mitochondrial iron-superoxide dismutase of Cryptosporidium parvum.Parasitology research · 2008Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundSuperoxide 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.
resultsThe 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.
conclusionThe 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.
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