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

Summary for 5JLG

• Entry DOI: 10.2210/pdb5jlg/pdb
• Descriptor: Ribonuclease pancreatic, RUTHENIUM ION, methyl (2Z)-3-hydroxy-3-(3-hydroxyphenyl)prop-2-ene(dithioate), ... (5 entities in total)
• Functional Keywords: ruthenated protein, protein-ru compound adducts, hydrolase, piano-stool organometallic ru(ii) arene compounds
• Biological source: Bos taurus (Cattle)
• Cellular location: Secreted: P61823
• Total number of polymer chains: 2
• Total formula weight: 28305.82

Authors

Ferraro, G.,Merlino, A. (deposition date: 2016-04-27, release date: 2016-08-03, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.79 Å)