9GGO
Strand-swapped dimer of engineered copper binding SH3-like protein
Summary for 9GGO
| Entry DOI | 10.2210/pdb9ggo/pdb |
| Descriptor | SH3-like protein, COPPER (II) ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | protein design, metal binding site, sh3-like domain, metal binding protein |
| Biological source | Homo sapiens |
| Total number of polymer chains | 1 |
| Total formula weight | 7064.91 |
| Authors | Schwan, M.,Kopp, J.,Sinning, I. (deposition date: 2024-08-13, release date: 2025-01-15, Last modification date: 2025-02-05) |
| Primary citation | Hage, F.R.,Schwan, M.,Conde Gonzalez, M.R.,Huber, J.,Germer, S.,Macri, M.,Kopp, J.,Sinning, I.,Thomas, F. Strand-Swapped SH3 Domain Dimer with Superoxide Dismutase Activity. Acs Cent.Sci., 11:157-166, 2025 Cited by PubMed Abstract: The design of metalloproteins allows us to better understand metal complexation in proteins and the resulting function. In this study, we incorporated a Cu-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. PubMed: 39866698DOI: 10.1021/acscentsci.4c01347 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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