4f2n

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<StructureSection load='4f2n' size='340' side='right' caption='[[4f2n]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='4f2n' size='340' side='right' caption='[[4f2n]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4f2n]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F2N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4f2n]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Leima Leima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F2N FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FESODA, LMJF_08_0290 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5664 Leishmania major])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FESODA, LMJF_08_0290 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5664 LEIMA])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f2n RCSB], [http://www.ebi.ac.uk/pdbsum/4f2n PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f2n RCSB], [http://www.ebi.ac.uk/pdbsum/4f2n PDBsum]</span></td></tr>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q4QIE0_LEIMA Q4QIE0_LEIMA]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]
[[http://www.uniprot.org/uniprot/Q4QIE0_LEIMA Q4QIE0_LEIMA]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]
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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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</div>
==See Also==
==See Also==
*[[Superoxide Dismutase|Superoxide Dismutase]]
*[[Superoxide Dismutase|Superoxide Dismutase]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Leishmania major]]
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[[Category: Leima]]
[[Category: Superoxide dismutase]]
[[Category: Superoxide dismutase]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

Revision as of 06:37, 3 June 2015

Crystal structure of iron superoxide dismutase from Leishmania major

4f2n, resolution 1.85Å

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