7YRK

Crystal structure of the hen egg lysozyme-2-oxidobenzylidene-threoninato-copper (II) complex

7YRK の概要

• エントリーDOI: 10.2210/pdb7yrk/pdb
• 分子名称: Lysozyme C, 1,2-ETHANEDIOL, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: complex, enzyme, lysozyme, activity, hydrolase
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16891.36

構造登録者

Unno, M.,Furuya, T.,Kitanishi, K.,Akitsu, T. (登録日: 2022-08-10, 公開日: 2023-05-10, 最終更新日: 2024-09-25)

主引用文献

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

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: 37106030
DOI: 10.1038/s41598-023-33926-1

実験手法

X-RAY DIFFRACTION (0.92 Å)