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Strand-swapped SH3 fomain fimer with superoxide dismutase activity [data]

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...

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Autori principali: Thomas, Franziska (Autore) , Häge, Florian (Autore) , Schwan, Merlin (Autore) , Conde González, Marcos Rafael (Autore) , Huber, Jonas (Autore) , Germer, Stefan (Autore) , Macrì, Matilde (Autore) , Kopp, Jürgen (Autore) , Sinning, Irmgard (Autore)
Natura: Database Research Data
Lingua:inglese
Pubblicazione: Heidelberg Universität 2026-07-06
DOI:10.11588/DATA/QSBCRU
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Accesso online:Verlag, kostenfrei, Volltext: https://doi.org/10.11588/DATA/QSBCRU
Verlag, kostenfrei, Volltext: https://heidata.uni-heidelberg.de/dataset.xhtml?persistentId=doi:10.11588/DATA/QSBCRU
Testo
Note sull'autore:Franziska Thomas, Florian Raphael Häge, Merlin Schwan, Marcos Rafael Conde González, Jonas Huber, Stefan Germer, Matilde Macrì, Jürgen Kopp, Irmgard Sinning
Descrizione
Riassunto: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.
Descrizione del documento:Gefördert durch: Deutsche Forschungsgemeinschaft: EXC-2082/1-390761711; Carl-Zeiss-Stiftung; Deutsche Forschungsgemeinschaft: INST 35/1314-1 FUGG; Deutsche Forschungsgemeinschaft: INST 35/1503-1 FUGG; Deutsche Forschungsgemeinschaft: INST 35/1597-1 FUGG; Ministerium für Wissenschaft, Forschung und Kunst Baden-Württemberg: INST 35/1314-1 FUGG; Ministerium für Wissenschaft, Forschung und Kunst Baden-Württemberg: INST 35/1503-1 FUGG; Ministerium für Wissenschaft, Forschung und Kunst Baden-Württemberg: INST 35/1314-1 FUGG; Bundesministerium für Bildung und Forschung: Max Planck School 'Matter to Life'; Max-Planck-Gesellschaft: Max Planck School 'Matter to Life'
Gesehen am 08.07.2026
Descrizione fisica:Online Resource
DOI:10.11588/DATA/QSBCRU

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