|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4yet' size='340' side='right'caption='[[4yet]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='4yet' size='340' side='right'caption='[[4yet]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yet]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Babbo Babbo]. 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> | + | <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> |
| - | </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> | + | </td></tr><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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k2w|4k2w]]</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=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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fe-SOD, BBOV_IV011480 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5865 BABBO])</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=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> | + | |
| | </table> | | </table> |
| | == 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). | + | [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). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 20: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Superoxide Dismutase|Superoxide Dismutase]] | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Babbo]] | + | [[Category: Babesia bovis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Superoxide dismutase]]
| + | [[Category: Abendroth J]] |
| - | [[Category: Abendroth, J]] | + | [[Category: Clifton MC]] |
| - | [[Category: Clifton, M C]] | + | [[Category: Edwards TE]] |
| - | [[Category: Edwards, T E]] | + | [[Category: Fairman JW]] |
| - | [[Category: Fairman, J W]] | + | [[Category: Lorimer D]] |
| - | [[Category: Lorimer, D]] | + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Ssgcid]]
| + | |
| Structural highlights
Function
O15904_BABBO Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Phan IQ, Davies DR, Moretti NS, Shanmugam D, Cestari I, Anupama A, Fairman JW, Edwards TE, Stuart K, Schenkman S, Myler PJ. Iron superoxide dismutases in eukaryotic pathogens: new insights from Apicomplexa and Trypanosoma structures. Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):615-21. doi:, 10.1107/S2053230X15004185. Epub 2015 May 7. PMID:25961325 doi:http://dx.doi.org/10.1107/S2053230X15004185
|
