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- W4382011218 abstract "Superoxide dismutase (SOD) is an essential and ubiquitous antioxidant protein that is widely present in biological systems. The anhydrobiotic tardigrades are some of the toughest micro-animals. They have an expanded set of genes for antioxidant proteins such as SODs. These proteins are thought to play an essential role in oxidative stress resistance in critical situations such as desiccation, although their functions at the molecular level have yet to be explored. Here, crystal structures of a copper/zinc-containing SOD ( Rv SOD15) from an anhydrobiotic tardigrade, Ramazzottius varieornatus strain YOKOZUNA-1, are reported. In Rv SOD15, one of the histidine ligands of the catalytic copper center is replaced by a valine (Val87). The crystal structures of the wild type and the V87H mutant show that even though a histidine is placed at position 87, a nearby flexible loop can destabilize the coordination of His87 to the Cu atom. Model structures of other Rv SODs were investigated and it was found that some of them are also unusual SODs, with features such as deletion of the electrostatic loop or β3 sheet and unusual metal-binding residues. These studies show that Rv SOD15 and some other Rv SODs may have evolved to lose the SOD function, suggesting that gene duplications of antioxidant proteins do not solely explain the high stress tolerance of anhydrobiotic tardigrades." @default.
- W4382011218 created "2023-06-27" @default.
- W4382011218 creator A5002998106 @default.
- W4382011218 creator A5004349096 @default.
- W4382011218 date "2023-06-26" @default.
- W4382011218 modified "2023-10-16" @default.
- W4382011218 title "Structure of a superoxide dismutase from a tardigrade: <i>Ramazzottius varieornatus</i> strain YOKOZUNA-1" @default.
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- W4382011218 doi "https://doi.org/10.1107/s2053230x2300523x" @default.
- W4382011218 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37358501" @default.
- W4382011218 hasPublicationYear "2023" @default.
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