| Full text | |
| Author(s): Show less - |
Phan, Isabelle Q. H.
;
Davies, Douglas R.
;
Moretti, Nilmar Silvio
;
Shanmugam, Dhanasekaran
;
Cestari, Igor
;
Anupama, Atashi
;
Fairman, James W.
;
Edwards, Thomas E.
;
Stuart, Kenneth
;
Schenkman, Sergio
;
Myler, Peter J.
Total Authors: 11
|
| Document type: | Journal article |
| Source: | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS; v. 71, p. 7-pg., 2015-05-01. |
| Abstract | |
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) | |
| FAPESP's process: | 13/20074-9 - Global analysis of protein acetylation in Trypanosoma cruzi |
| Grantee: | Nilmar Silvio Moretti |
| Support Opportunities: | Scholarships abroad - Research Internship - Post-doctor |
| FAPESP's process: | 11/51973-3 - Cell signaling mechanism of Trypanosoma in response to nutritional alterations and genotoxic agents |
| Grantee: | Sergio Schenkman |
| Support Opportunities: | Research Projects - Thematic Grants |