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| | ==Candida albicans Superoxide Dismutase 5 (SOD5), Cu(II)== | | ==Candida albicans Superoxide Dismutase 5 (SOD5), Cu(II)== |
| - | <StructureSection load='4n3u' size='340' side='right' caption='[[4n3u]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='4n3u' size='340' side='right'caption='[[4n3u]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n3u]] 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=4N3U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N3U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n3u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_SC5314 Candida albicans SC5314]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N3U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n3t|4n3t]]</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=4n3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n3u OCA], [https://pdbe.org/4n3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n3u RCSB], [https://www.ebi.ac.uk/pdbsum/4n3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n3u ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CaO19.2060, CaO19.9607, SOD31, SOD5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237561 CANAL])</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=4n3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n3u OCA], [http://pdbe.org/4n3u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n3u RCSB], [http://www.ebi.ac.uk/pdbsum/4n3u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n3u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SOD5_CANAL 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.<ref>PMID:14617819</ref> <ref>PMID:19019164</ref> <ref>PMID:21746956</ref> | + | [https://www.uniprot.org/uniprot/SOD5_CANAL 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.<ref>PMID:14617819</ref> <ref>PMID:19019164</ref> <ref>PMID:21746956</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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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: Candida albicans SC5314]] |
| - | [[Category: Galaleldeen, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Hart, P J]] | + | [[Category: Galaleldeen A]] |
| - | [[Category: Holloway, S P]] | + | [[Category: Hart PJ]] |
| - | [[Category: Taylor, A B]] | + | [[Category: Holloway SP]] |
| - | [[Category: Waninger-Saroni, J J]] | + | [[Category: Taylor AB]] |
| - | [[Category: Antioxidant]]
| + | [[Category: Waninger-Saroni JJ]] |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Oxidative burst]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Zinc loop]]
| + | |
| Structural highlights
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
The human fungal pathogens Candida albicans and Histoplasma capsulatum have been reported to protect against the oxidative burst of host innate immune cells using a family of extracellular proteins with similarity to Cu/Zn superoxide dismutase 1 (SOD1). We report here that these molecules are widespread throughout fungi and deviate from canonical SOD1 at the primary, tertiary, and quaternary levels. The structure of C. albicans SOD5 reveals that although the beta-barrel of Cu/Zn SODs is largely preserved, SOD5 is a monomeric copper protein that lacks a zinc-binding site and is missing the electrostatic loop element proposed to promote catalysis through superoxide guidance. Without an electrostatic loop, the copper site of SOD5 is not recessed and is readily accessible to bulk solvent. Despite these structural deviations, SOD5 has the capacity to disproportionate superoxide with kinetics that approach diffusion limits, similar to those of canonical SOD1. In cultures of C. albicans, SOD5 is secreted in a disulfide-oxidized form and apo-pools of secreted SOD5 can readily capture extracellular copper for rapid induction of enzyme activity. We suggest that the unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface.
Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense.,Gleason JE, Galaleldeen A, Peterson RL, Taylor AB, Holloway SP, Waninger-Saroni J, Cormack BP, Cabelli DE, Hart PJ, Culotta VC Proc Natl Acad Sci U S A. 2014 Apr 22;111(16):5866-71. doi:, 10.1073/pnas.1400137111. Epub 2014 Apr 7. PMID:24711423[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
- ↑ Gleason JE, Galaleldeen A, Peterson RL, Taylor AB, Holloway SP, Waninger-Saroni J, Cormack BP, Cabelli DE, Hart PJ, Culotta VC. Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense. Proc Natl Acad Sci U S A. 2014 Apr 22;111(16):5866-71. doi:, 10.1073/pnas.1400137111. Epub 2014 Apr 7. PMID:24711423 doi:http://dx.doi.org/10.1073/pnas.1400137111
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