7YRK
Crystal structure of the hen egg lysozyme-2-oxidobenzylidene-threoninato-copper (II) complex
Summary for 7YRK
| Entry DOI | 10.2210/pdb7yrk/pdb |
| Descriptor | Lysozyme C, 1,2-ETHANEDIOL, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | complex, enzyme, lysozyme, activity, hydrolase |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 16891.36 |
| Authors | Unno, M.,Furuya, T.,Kitanishi, K.,Akitsu, T. (deposition date: 2022-08-10, release date: 2023-05-10, Last modification date: 2024-09-25) |
| Primary citation | Furuya, T.,Nakane, D.,Kitanishi, K.,Katsuumi, N.,Tsaturyan, A.,Shcherbakov, I.N.,Unno, M.,Akitsu, T. A novel hybrid protein composed of superoxide-dismutase-active Cu(II) complex and lysozyme. Sci Rep, 13:6892-6892, 2023 Cited by PubMed Abstract: A novel hybrid protein composed of a superoxide dismutase-active Cu(II) complex (CuST) and lysozyme (CuST@lysozyme) was prepared. The results of the spectroscopic and electrochemical analyses confirmed that CuST binds to lysozyme. We determined the crystal structure of CuST@lysozyme at 0.92 Å resolution, which revealed that the His15 imidazole group of lysozyme binds to the Cu(II) center of CuST in the equatorial position. In addition, CuST was fixed in position by the weak axial coordination of the Thr89 hydroxyl group and the hydrogen bond between the guanidinium group of the Arg14 residue and the hydroxyl group of CuST. Furthermore, the combination of CuST with lysozyme did not decrease the superoxide dismutase activity of CuST. Based on the spectral, electrochemical, structural studies, and quantum chemical calculations, an O disproportionation mechanism catalyzed by CuST@lysozyme is proposed. PubMed: 37106030DOI: 10.1038/s41598-023-33926-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.92 Å) |
Structure validation
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