4yet

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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/O15904_BABBO O15904_BABBO]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).
[[http://www.uniprot.org/uniprot/O15904_BABBO O15904_BABBO]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Iron superoxide dismutases in eukaryotic pathogens: new insights from Apicomplexa and Trypanosoma structures.,Phan IQ, Davies DR, Moretti NS, Shanmugam D, Cestari I, Anupama A, Fairman JW, Edwards TE, Stuart K, Schenkman S, Myler PJ Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):615-21. doi:, 10.1107/S2053230X15004185. Epub 2015 May 7. PMID:25961325<ref>PMID:25961325</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 06:57, 3 June 2015

X-ray crystal structure of superoxide dismutase from Babesia bovis solved by Sulfur SAD

4yet, resolution 1.75Å

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