4H3E

Crystal structure of a putative iron superoxide dismutase from Trypanosoma cruzi bound to iron

Summary for 4H3E

• Entry DOI: 10.2210/pdb4h3e/pdb
• Related: 4F2N
• Descriptor: Superoxide dismutase, FE (II) ION (3 entities in total)
• Functional Keywords: structural genomics, niaid, national institute of allergy and infectious diseases, seattle structural genomics center for infectious disease, ssgcid, radical oxygen species, trypanosomiasis, parasitic euglenoid trypanosome, chagas disease, radical scavenger, hydrogen peroxide, antioxidant, oxidoreductase
• Biological source: Trypanosoma cruzi
• Total number of polymer chains: 2
• Total formula weight: 54589.93

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-09-13, release date: 2012-09-26, Last modification date: 2023-09-20)

Primary citation

Phan, I.Q.,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.
Iron superoxide dismutases in eukaryotic pathogens: new insights from Apicomplexa and Trypanosoma structures.
Acta Crystallogr F Struct Biol Commun, 71:615-621, 2015

PubMed 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.

PubMed: 25961325
DOI: 10.1107/S2053230X15004185

Experimental method

X-RAY DIFFRACTION (2.25 Å)