4YET
X-ray crystal structure of superoxide dismutase from Babesia bovis solved by Sulfur SAD
Replaces: 4K2WSummary for 4YET
| Entry DOI | 10.2210/pdb4yet/pdb |
| Related | 4K2W |
| Descriptor | Superoxide dismutase, FE (III) ION (3 entities in total) |
| Functional Keywords | superoxide dismutase, ssgcid, structural genomics, seattle structural genomics center for infectious disease, oxidoreductase |
| Biological source | Babesia bovis |
| Total number of polymer chains | 2 |
| Total formula weight | 45915.31 |
| Authors | Fairman, J.W.,Clifton, M.C.,Abendroth, J.,Edwards, T.E.,Lorimer, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2015-02-24, release date: 2015-04-15, Last modification date: 2024-02-28) |
| 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.,Sect.F, 71:615-621, 2015 Cited by 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: 25961325DOI: 10.1107/S2053230X15004185 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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