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4f2n
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4f2n]] is a 12 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4F2N FirstGlance]. <br> | <table><tr><td colspan='2'>[[4f2n]] is a 12 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4F2N FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2n OCA], [https://pdbe.org/4f2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f2n RCSB], [https://www.ebi.ac.uk/pdbsum/4f2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f2n ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2n OCA], [https://pdbe.org/4f2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f2n RCSB], [https://www.ebi.ac.uk/pdbsum/4f2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f2n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://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] | [https://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] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4f2n" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Leishmania major]] | [[Category: Leishmania major]] | ||
Current revision
Crystal structure of iron superoxide dismutase from Leishmania major
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