Structural highlights
FunctionQ9RYV4_DEIRA Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in favoring mycobacterial survival in phagocytes.[ARBA:ARBA00024900] Publication Abstract from PubMedCu/Zn-superoxide dismutase (Cu/Zn-SOD) is an antioxidant enzyme widely present across species; however, the structural diversity and physiological roles of Cu/Zn-SOD are yet to be fully uncovered. Here, we show a unique type of Cu/Zn-SOD from Deinococcus radiodurans (DrSOD) with an additional beta-propeller domain. Our structural analysis of DrSOD revealed a typical bacterial Cu/Zn-SOD domain, binding both a copper and zinc ion, alongside a six-bladed beta-propeller domain coordinating a calcium ion. DrSOD was indeed expressed in D. radiodurans, but its deletion did not lead to any noticeable changes in resistance to DNA-damaging stresses, a characteristic trait of D. radiodurans. Despite this, the Cu/Zn-SOD domain retained superoxide dismutase activity, and the beta-propeller domain was found to exhibit a lactonase activity specifically for hydrolyzing 2-coumaranone. Taken together, while the precise physiological role of DrSOD needs to be further investigated, our findings here reveal a unique multi-functional enzyme architecture, expanding the known structural diversity of Cu/Zn-SODs. Cu/Zn-superoxide dismutase naturally fused with a beta-propeller lactonase in Deinococcus radiodurans.,Furukawa Y, Megata M, Shintani A, Sue K, Morohoshi T, Akutsu M, Muraki N J Biol Chem. 2025 Aug;301(8):110499. doi: 10.1016/j.jbc.2025.110499. Epub 2025 , Jul 18. PMID:40684944[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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