5JLG

The X-ray structure of the adduct formed in the reaction between bovine pancreatic ribonuclease and compound I, a piano-stool organometallic Ru(II) arene compound containing an O,S-chelating ligand

5JLG の概要

• エントリーDOI: 10.2210/pdb5jlg/pdb
• 分子名称: Ribonuclease pancreatic, RUTHENIUM ION, methyl (2Z)-3-hydroxy-3-(3-hydroxyphenyl)prop-2-ene(dithioate), ... (5 entities in total)
• 機能のキーワード: ruthenated protein, protein-ru compound adducts, hydrolase, piano-stool organometallic ru(ii) arene compounds
• 由来する生物種: Bos taurus (Cattle)
• 細胞内の位置: Secreted: P61823
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28305.82

構造登録者

Ferraro, G.,Merlino, A. (登録日: 2016-04-27, 公開日: 2016-08-03, 最終更新日: 2024-10-23)

主引用文献

Hildebrandt, J.,Gorls, H.,Hafner, N.,Ferraro, G.,Durst, M.,Runnebaum, I.B.,Weigand, W.,Merlino, A.
Unusual mode of protein binding by a cytotoxic pi-arene ruthenium(ii) piano-stool compound containing an O,S-chelating ligand.
Dalton Trans, 45:12283-12287, 2016

PubMed Abstract: A new pseudo-octahedral π-arene ruthenium(ii) piano-stool compound, containing an O,S-bidentate ligand (compound 1) and showing significant cytotoxic activity in vitro, was synthesized and characterized. In solution stability and interaction with the model protein bovine pancreatic ribonuclease (RNase A) were investigated by using UV-Vis absorption spectroscopy. Its crystal structure and that of the adduct formed upon reaction with RNase A were obtained by X-ray crystallography. The comparison between the structure of purified compound 1 and that of the fragment bound to RNase A reveals an unusual mode of protein binding that includes ligand exchange and alteration of coordination sphere geometry.

PubMed: 27427335
DOI: 10.1039/c6dt02380k

実験手法

X-RAY DIFFRACTION (1.79 Å)