7b4o: Difference between revisions
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==A Bacteroidetes bacterium CuZn-superoxide dismutase with ZnZn metalation== | ==A Bacteroidetes bacterium CuZn-superoxide dismutase with ZnZn metalation== | ||
<StructureSection load='7b4o' size='340' side='right'caption='[[7b4o]]' scene=''> | <StructureSection load='7b4o' size='340' side='right'caption='[[7b4o]], [[Resolution|resolution]] 1.41Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B4O FirstGlance]. <br> | <table><tr><td colspan='2'>[[7b4o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroidetes_bacterium_gwa2_30_7 Bacteroidetes bacterium gwa2_30_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B4O FirstGlance]. <br> | ||
</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=7b4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b4o OCA], [https://pdbe.org/7b4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b4o RCSB], [https://www.ebi.ac.uk/pdbsum/7b4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b4o ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A2046_17220 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1797313 Bacteroidetes bacterium GWA2_30_7])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7b4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b4o OCA], [https://pdbe.org/7b4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b4o RCSB], [https://www.ebi.ac.uk/pdbsum/7b4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b4o ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/A0A1F3DVA5_9BACT A0A1F3DVA5_9BACT]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000393] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Internalisation of a bacteria by an archaeal cell expedited eukaryotic evolution. An important feature of the species that diversified into the great variety of eukaryotic life visible today was the ability to combat oxidative stress with a copper-zinc superoxide dismutase (CuZnSOD) enzyme activated by a specific, high affinity copper chaperone. Adoption of a single protein interface that facilitates homodimerisation and heterodimerisation was essential, however, its evolution has been difficult to rationalise given the structural differences between bacterial and eukaryotic enzymes. In contrast, no consistent strategy for the maturation of periplasmic bacterial CuZnSODs has emerged. Here, 34 copper-zinc superoxide dismutases are described that closely resemble the eukaryotic form but originate predominantly from aquatic bacteria. Crystal structures of a Bacteroidetes bacterium copper-zinc superoxide dismutase portray both prokaryotic and eukaryotic characteristics and propose a mechanism for self-catalysed disulphide maturation. Unification of a bacterial but eukaryotic-like CuZnSOD along with a ferredoxin-fold MXCXXC copper binding domain within a single polypeptide created the advanced copper delivery system for CuZnSODs exemplified by the human copper chaperone for superoxide dismutase-1. The development of this system facilitated evolution of large and compartmentalised cells following endosymbiotic eukaryogenesis. | |||
Bacterial evolutionary precursors of eukaryotic copper-zinc superoxide dismutases.,Wright GSA Mol Biol Evol. 2021 May 22. pii: 6281076. doi: 10.1093/molbev/msab157. PMID:34021750<ref>PMID:34021750</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7b4o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacteroidetes bacterium gwa2_30_7]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Wright | [[Category: Superoxide dismutase]] | ||
[[Category: Wright, G S.A]] | |||
[[Category: Bacterial]] | |||
[[Category: Copper]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Zinc]] | |||
Revision as of 11:59, 29 September 2021
A Bacteroidetes bacterium CuZn-superoxide dismutase with ZnZn metalationA Bacteroidetes bacterium CuZn-superoxide dismutase with ZnZn metalation
Structural highlights
Function[A0A1F3DVA5_9BACT] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000393] Publication Abstract from PubMedInternalisation of a bacteria by an archaeal cell expedited eukaryotic evolution. An important feature of the species that diversified into the great variety of eukaryotic life visible today was the ability to combat oxidative stress with a copper-zinc superoxide dismutase (CuZnSOD) enzyme activated by a specific, high affinity copper chaperone. Adoption of a single protein interface that facilitates homodimerisation and heterodimerisation was essential, however, its evolution has been difficult to rationalise given the structural differences between bacterial and eukaryotic enzymes. In contrast, no consistent strategy for the maturation of periplasmic bacterial CuZnSODs has emerged. Here, 34 copper-zinc superoxide dismutases are described that closely resemble the eukaryotic form but originate predominantly from aquatic bacteria. Crystal structures of a Bacteroidetes bacterium copper-zinc superoxide dismutase portray both prokaryotic and eukaryotic characteristics and propose a mechanism for self-catalysed disulphide maturation. Unification of a bacterial but eukaryotic-like CuZnSOD along with a ferredoxin-fold MXCXXC copper binding domain within a single polypeptide created the advanced copper delivery system for CuZnSODs exemplified by the human copper chaperone for superoxide dismutase-1. The development of this system facilitated evolution of large and compartmentalised cells following endosymbiotic eukaryogenesis. Bacterial evolutionary precursors of eukaryotic copper-zinc superoxide dismutases.,Wright GSA Mol Biol Evol. 2021 May 22. pii: 6281076. doi: 10.1093/molbev/msab157. PMID:34021750[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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