Iron superoxide dismutases in eukaryotic pathogens: new insights from Apicomplexa and Trypanosoma structures

This report presents the structures of three iron-dependent superoxide dismutases (FeSODs) from Trypanosoma cruzi, Leishmania major and Babesia bovis. Comparison with existing structures from Plasmodium and other trypanosome isoforms shows a very conserved overall fold with subtle differences. In particular, structural data suggest that B. bovis FeSOD may display similar resistance to peroxynitrite-mediated inactivation via an intramolecular electron-transfer pathway as previously described in T. cruzi FeSOD isoform B, thus providing valuable information for structure-based drug design. Furthermore, lysine-acetylation results in T. cruzi indicate that acetylation occurs at a position close to that responsible for the regulation of acetylation-mediated activity in the human enzyme.

Source: Acta Crystallographica Section F - May 7, 2015 Category: Biochemistry Authors: Phan, I.Q.H.Davies, D.R.Moretti, N.S.Shanmugam, D.Cestari, I.Anupama, A.Fairman, J.W.Edwards, T.E.Stuart, K.Schenkman, S.Myler, P.J. Tags: iron superoxide dismutase Trypanosoma Apicomplexa research communications Source Type: research