4F2N

Crystal structure of iron superoxide dismutase from Leishmania major

Summary for 4F2N

• Entry DOI: 10.2210/pdb4f2n/pdb
• Descriptor: Superoxide dismutase, FE (II) ION (3 entities in total)
• Functional Keywords: ssgcid, nih, niaid, sbri, emerald biostructures, structural genomics, national institute of allergy and infectious diseases, seattle structural genomics center for infectious disease, oxidoreductase
• Biological source: Leishmania major
• Total number of polymer chains: 12
• Total formula weight: 313938.97

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-05-08, release date: 2012-05-16, Last modification date: 2023-09-13)

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 (1.85 Å)