Strand-swapped SH3 domain dimer with superoxide dismutase activity
The design of metalloproteins allows us to better understand metal complexation in proteins and the resulting function. In this study, we incorporated a Cu2+-binding site into a natural protein domain, the 58 amino acid c-Crk-SH3, to create a miniaturized superoxide dismutase model, termed SO1. The...
Gespeichert in:
| Hauptverfasser: | , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
January 10, 2025
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| In: |
ACS central science
Year: 2025, Jahrgang: 11, Heft: 1, Pages: 157-166 |
| ISSN: | 2374-7951 |
| DOI: | 10.1021/acscentsci.4c01347 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: https://doi.org/10.1021/acscentsci.4c01347 Verlag, kostenfrei, Volltext: https://pubs.acs.org/doi/10.1021/acscentsci.4c01347 
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| Verfasserangaben: | Florian R. Häge, Merlin Schwan, Marcos Rafael Conde González, Jonas Huber, Stefan Germer, Matilde Macrì, Jürgen Kopp, Irmgard Sinning, and Franziska Thomas |
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| 245 | 1 | 0 | |a Strand-swapped SH3 domain dimer with superoxide dismutase activity |c Florian R. Häge, Merlin Schwan, Marcos Rafael Conde González, Jonas Huber, Stefan Germer, Matilde Macrì, Jürgen Kopp, Irmgard Sinning, and Franziska Thomas |
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| 520 | |a The design of metalloproteins allows us to better understand metal complexation in proteins and the resulting function. In this study, we incorporated a Cu2+-binding site into a natural protein domain, the 58 amino acid c-Crk-SH3, to create a miniaturized superoxide dismutase model, termed SO1. The resulting low complexity metalloprotein was characterized for structure and function by circular dichroism and UV spectroscopy as well as EPR spectroscopy and X-ray crystallography. The miniprotein was found to be a strand-swapped dimer with an unusual coupled binuclear Type 2-like copper center in each protomer. SO1-Cu was found to be SOD-active with an activity only 1 order of magnitude lower than that of natural SOD enzymes and 1 to 2 orders of magnitude higher than that of other low-complexity SOD protein models of similar size. This serendipitous design provides us with a new structural template for future designs of binuclear metalloproteins with different metal ions and functions. | ||
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