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| | ==Candida Albicans Superoxide Dismutase 5 (SOD5), D113N Mutant== | | ==Candida Albicans Superoxide Dismutase 5 (SOD5), D113N Mutant== |
| - | <StructureSection load='5kbm' size='340' side='right' caption='[[5kbm]], [[Resolution|resolution]] 1.42Å' scene=''> | + | <StructureSection load='5kbm' size='340' side='right'caption='[[5kbm]], [[Resolution|resolution]] 1.42Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5kbm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KBM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5kbm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canal Canal]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KBM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KBM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kbl|5kbl]], [[5kbk|5kbk]]</td></tr> | | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kbl|5kbl]], [[5kbk|5kbk]]</td></tr> |
| | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SOD5, PGA3, SOD31, CaO19.2060, CaO19.9607 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237561 CANAL])</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=5kbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kbm OCA], [http://pdbe.org/5kbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kbm RCSB], [http://www.ebi.ac.uk/pdbsum/5kbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kbm ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5kbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kbm OCA], [http://pdbe.org/5kbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kbm RCSB], [http://www.ebi.ac.uk/pdbsum/5kbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kbm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
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| | ==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: Canal]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Superoxide dismutase]] | | [[Category: Superoxide dismutase]] |
| | [[Category: Galaleldeen, A]] | | [[Category: Galaleldeen, A]] |
| Structural highlights
5kbm is a 1 chain structure with sequence from Canal. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Related: | 5kbl, 5kbk |
| Gene: | SOD5, PGA3, SOD31, CaO19.2060, CaO19.9607 (CANAL) |
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[SOD5_CANAL] Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action. Degrades host-derived reactive oxygen species to escape innate immune surveillance. Involved in the occurrence of miconazole-tolerant persisters in biofilms. Persisters are cells that survive high doses of an antimicrobial agent.[1] [2] [3]
Publication Abstract from PubMed
In eukaryotes, the bimetallic Cu/Zn superoxide dismutase (SOD) enzymes play important roles in the biology of reactive oxygen species by disproportionating superoxide anion. Recently, we reported that the fungal pathogen Candida albicans expresses a novel Cu-only SOD known as SOD5, that lacks the Zn cofactor and electrostatic loop (ESL) domain of Cu/Zn SODs for substrate guidance. Despite these abnormalities, C. albicans SOD5 can disproportionate superoxide at rates limited only by diffusion. Here we demonstrate that this curious Cu-only SOD occurs throughout the fungal kingdom as well as in phylogenetically distant oomycetes or pseudofungi species. It is the only form of extracellular SOD in fungi and oomycetes, in stark contrast to the extracellular Cu/Zn SODs of plants and animals. Through structural biology and biochemical approaches we demonstrate that these Cu-only SODs have evolved with a specialized active site consisting of two highly conserved residues equivalent to SOD5 E110 and D113. The equivalent positions are Zn binding ligands in Cu/Zn SODs and have evolved in Cu-only SODs to control catalysis and Cu binding in lieu of Zn and the ESL. Similar to the Zn ion in Cu/Zn SODs, SOD5 E110 helps orients a key Cu coordinating histidine and extends the pH range of enzyme catalysis. SOD5 D113 connects to the active site in a manner similar to that of the ESL in Cu/Zn SODs and assists in Cu cofactor binding. Cu-only SODs are virulence factors for certain fungal pathogens; thus this unique active site may be a target for future anti-fungal strategies.
The Phylogeny and Active Site Design of Eukaryotic Cu-only Superoxide Dismutases.,Peterson RL, Galaleldeen A, Villarreal J, Taylor AB, Cabelli DE, Hart PJ, Culotta VC J Biol Chem. 2016 Aug 17. pii: jbc.M116.748251. PMID:27535222[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Martchenko M, Alarco AM, Harcus D, Whiteway M. Superoxide dismutases in Candida albicans: transcriptional regulation and functional characterization of the hyphal-induced SOD5 gene. Mol Biol Cell. 2004 Feb;15(2):456-67. Epub 2003 Nov 14. PMID:14617819 doi:http://dx.doi.org/10.1091/mbc.E03-03-0179
- ↑ Frohner IE, Bourgeois C, Yatsyk K, Majer O, Kuchler K. Candida albicans cell surface superoxide dismutases degrade host-derived reactive oxygen species to escape innate immune surveillance. Mol Microbiol. 2009 Jan;71(1):240-52. doi: 10.1111/j.1365-2958.2008.06528.x. Epub, 2008 Nov 4. PMID:19019164 doi:http://dx.doi.org/10.1111/j.1365-2958.2008.06528.x
- ↑ Bink A, Vandenbosch D, Coenye T, Nelis H, Cammue BP, Thevissen K. Superoxide dismutases are involved in Candida albicans biofilm persistence against miconazole. Antimicrob Agents Chemother. 2011 Sep;55(9):4033-7. doi: 10.1128/AAC.00280-11., Epub 2011 Jul 11. PMID:21746956 doi:http://dx.doi.org/10.1128/AAC.00280-11
- ↑ Peterson RL, Galaleldeen A, Villarreal J, Taylor AB, Cabelli DE, Hart PJ, Culotta VC. The Phylogeny and Active Site Design of Eukaryotic Cu-only Superoxide Dismutases. J Biol Chem. 2016 Aug 17. pii: jbc.M116.748251. PMID:27535222 doi:http://dx.doi.org/10.1074/jbc.M116.748251
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