8avk
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8avk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Wolfebacteria_bacterium_GW2011_GWB1_47_1 Candidatus Wolfebacteria bacterium GW2011_GWB1_47_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AVK FirstGlance]. <br> | <table><tr><td colspan='2'>[[8avk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Wolfebacteria_bacterium_GW2011_GWB1_47_1 Candidatus Wolfebacteria bacterium GW2011_GWB1_47_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AVK FirstGlance]. <br> | ||
- | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8avk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8avk OCA], [https://pdbe.org/8avk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8avk RCSB], [https://www.ebi.ac.uk/pdbsum/8avk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8avk ProSAT]</span></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=8avk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8avk OCA], [https://pdbe.org/8avk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8avk RCSB], [https://www.ebi.ac.uk/pdbsum/8avk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8avk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A0G1X6V3_9BACT A0A0G1X6V3_9BACT] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] | [https://www.uniprot.org/uniprot/A0A0G1X6V3_9BACT A0A0G1X6V3_9BACT] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Evolution creates functional diversity of proteins, the essential building blocks of all biological systems. However, studies of natural proteins sampled across the tree of life and evaluated in a single experimental system are lacking. Almost half of enzymes require metals, and metalloproteins tend to optimally utilize the physicochemical properties of a specific metal co-factor. Life must adapt to changes in metal bioavailability, including those during the transition from anoxic to oxic Earth or pathogens' exposure to nutritional immunity. These changes can challenge the ability of metalloenzymes to maintain activity, presumptively driving their evolution. Here we studied metal-preference evolution within the natural diversity of the iron/manganese superoxide dismutase (SodFM) family of reactive oxygen species scavengers. We identified and experimentally verified residues with conserved roles in determining metal preference that, when combined with an understanding of the protein's evolutionary history, improved prediction of metal utilization across the five SodFM subfamilies defined herein. By combining phylogenetics, biochemistry and structural biology, we demonstrate that SodFM metal utilization can be evolutionarily fine tuned by sliding along a scale between perfect manganese and iron specificities. Over the history of life, SodFM metal preference has been modulated multiple independent times within different evolutionary and ecological contexts, and can be changed within short evolutionary timeframes. | ||
- | + | ==See Also== | |
- | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Superoxide dismutase SodFM1 from CPR Parkubacteria Wolfebacteria
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