Phan, Isabelle Q. H.
Davies, Douglas R.
Moretti, Nilmar Silvio
Fairman, James W.
Edwards, Thomas E.
Myler, Peter J.
Número total de Autores: 11
Afiliação do(s) autor(es):
 SSGCID, Seattle, WA 98109 - USA
 Seattle Biomed Res Inst, Seattle, WA 98109 - USA
 Beryllium, Bainbridge Isl, WA 98110 - USA
 Univ Fed Sao Paulo UNIFESP, Dept Microbiol Imunol & Parasitol, Sao Paulo - Brazil
 CSIR Natl Chem Lab, Pune 411008, Maharashtra - India
Número total de Afiliações: 5
Tipo de documento:
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS;
n. 5, SI,
Citações Web of Science:
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) 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. (AU)