3QE8

Crystal Structure Analysis of Lysozyme-bound fac-[Re(CO)3(H2O)(Im)]+

3QE8 の概要

• エントリーDOI: 10.2210/pdb3qe8/pdb
• 関連するPDBエントリー: 3QNG
• 分子名称: Lysozyme C, Tricarbonyl (aqua) (imidazole) rhenium(I), 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: hydrolase, rhenium complex, metallation
• 由来する生物種: Gallus gallus (Chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29605.47

構造登録者

Zobi, F.,Spingler, B. (登録日: 2011-01-20, 公開日: 2012-01-18, 最終更新日: 2024-10-30)

主引用文献

Zobi, F.,Spingler, B.
Post-protein-binding reactivity and modifications of the fac-[Re(CO)3]+ core
Inorg.Chem., 51:1210-1212, 2012

PubMed Abstract: The reactivity of the [Re(CO)(3)(H(2)O)(2)](+) complex coordinated to the His15 residue of HEW lysozyme is described. In the fully metalated protein (Lys-1), the Re ion retains its reactivity only toward selected ligands, while others induce a ligand-mediated demetalation of the enzyme. It is further shown that some of the complexes that may be "engineered" on the lysozyme do not react with the free protein even if present in solution in excess. The formation of stable metal adducts starting from Lys-1 was confirmed by X-ray crystallography.

PubMed: 22229733
DOI: 10.1021/ic2023314

実験手法

X-RAY DIFFRACTION (1.49 Å)