4yet

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==X-ray crystal structure of superoxide dismutase from Babesia bovis solved by Sulfur SAD==
==X-ray crystal structure of superoxide dismutase from Babesia bovis solved by Sulfur SAD==
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<StructureSection load='4yet' size='340' side='right' caption='[[4yet]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='4yet' size='340' side='right'caption='[[4yet]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4yet]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4k2w 4k2w]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YET FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4yet]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4k2w 4k2w]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YET FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k2w|4k2w]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yet OCA], [https://pdbe.org/4yet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yet RCSB], [https://www.ebi.ac.uk/pdbsum/4yet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yet ProSAT]</span></td></tr>
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<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=4yet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yet OCA], [http://pdbe.org/4yet PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yet RCSB], [http://www.ebi.ac.uk/pdbsum/4yet PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yet ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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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[https://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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</div>
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<div class="pdbe-citations 4yet" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Superoxide Dismutase|Superoxide Dismutase]]
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Superoxide dismutase]]
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[[Category: Babesia bovis]]
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[[Category: Abendroth, J]]
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[[Category: Large Structures]]
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[[Category: Clifton, M C]]
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[[Category: Abendroth J]]
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[[Category: Edwards, T E]]
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[[Category: Clifton MC]]
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[[Category: Fairman, J W]]
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[[Category: Edwards TE]]
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[[Category: Lorimer, D]]
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[[Category: Fairman JW]]
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[[Category: Structural genomic]]
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[[Category: Lorimer D]]
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[[Category: Oxidoreductase]]
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[[Category: Ssgcid]]
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Current revision

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

PDB ID 4yet

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