Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Combined Automated Annotation using Multiple IEA Methods
Structure of a superoxide dismutase from a tardigrade: Ramazzottius varieornatus strain YOKOZUNA-1.
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Crystal structures of RvSOD15 (PDB 7YPP, 7YPR) solved at 2.1-2.2 A resolution
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Homodimeric quaternary structure confirmed
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Copper and zinc binding confirmed in the structure
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Critical catalytic His ligand replaced by Val87 in wild-type protein
"In RvSOD15, one of the histidine ligands of the catalytic copper center is replaced by a valine (Val87)."
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V87H mutant structure shows flexible loop destabilizes His87 coordination to Cu
"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."
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Authors conclude RvSOD15 may have evolved to lose SOD function
"These studies show that RvSOD15 and some other RvSODs 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."
Extremotolerant tardigrade genome and improved radiotolerance of human cultured cells by tardigrade-unique protein.
OpenScientist focused review of RvY_13070 superoxide dismutase activity hypothesis
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OpenScientist judged the RvY_13070 superoxide dismutase activity hypothesis over-annotated.
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The report prioritized the RvSOD15 Val87 copper-ligand substitution, the V87H reversion-mutant structure, and cross-species Cu/Zn SOD active-site evidence as reasons to doubt catalytic SOD activity.
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The report recommended retaining copper and zinc binding annotations but flagging superoxide-removal process annotations for coordinated review with GO:0004784.