Publication Date:
2015-05-01
Description:
Prior studies have highlighted the potential of superoxide dismutases as drug targets in eukaryotic pathogens. This report presents the structures of three iron-dependent superoxide dismutases (FeSODs) fromTrypanosoma cruzi,Leishmania majorandBabesia bovis. Comparison with existing structures fromPlasmodiumand other trypanosome isoforms shows a very conserved overall fold with subtle differences. In particular, structural data suggest thatB. bovisFeSOD may display similar resistance to peroxynitrite-mediated inactivationviaan intramolecular electron-transfer pathway as previously described inT. cruziFeSOD isoform B, thus providing valuable information for structure-based drug design. Furthermore, lysine-acetylation results inT. cruziindicate that acetylation occurs at a position close to that responsible for the regulation of acetylation-mediated activity in the human enzyme.
Electronic ISSN:
2053-230X
Topics:
Biology
,
Chemistry and Pharmacology
,
Geosciences
,
Physics
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