4h3e
From Proteopedia
(Difference between revisions)
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<StructureSection load='4h3e' size='340' side='right' caption='[[4h3e]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='4h3e' size='340' side='right' caption='[[4h3e]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4h3e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4h3e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trycc Trycc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H3E 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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f2n|4f2n]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f2n|4f2n]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tc00.1047053509775.40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tc00.1047053509775.40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=353153 TRYCC])</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=4h3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h3e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h3e RCSB], [http://www.ebi.ac.uk/pdbsum/4h3e 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=4h3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h3e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h3e RCSB], [http://www.ebi.ac.uk/pdbsum/4h3e PDBsum]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/Q4DCQ3_TRYCC Q4DCQ3_TRYCC]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).[RuleBase:RU000414] | [[http://www.uniprot.org/uniprot/Q4DCQ3_TRYCC Q4DCQ3_TRYCC]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).[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. | ||
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
| - | [[Category: | + | [[Category: Trycc]] |
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Antioxidant]] | [[Category: Antioxidant]] | ||
Revision as of 07:03, 3 June 2015
Crystal structure of a putative iron superoxide dismutase from Trypanosoma cruzi bound to iron
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