6QEA
The X-ray structure of the adduct formed in the reaction between hen egg white lysozyme and complex I, a pentacoordinate Pt(II) compound containing 2,9-dimethyl-1,10-phenanthroline, dimethylfumarate, methyl and iodine as ligands
Summary for 6QEA
| Entry DOI | 10.2210/pdb6qea/pdb |
| Descriptor | Lysozyme C, NITRATE ION, pentacoordinate Pt(II) compound, ... (5 entities in total) |
| Functional Keywords | five-coordinate pt complexes, anticancer platinum compounds, protein metal coordination, lyase |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 15178.74 |
| Authors | Merlino, A.,Ferraro, G. (deposition date: 2019-01-07, release date: 2019-03-27, Last modification date: 2024-01-24) |
| Primary citation | Ferraro, G.,Marzo, T.,Cucciolito, M.E.,Ruffo, F.,Messori, L.,Merlino, A. Reaction with Proteins of a Five-Coordinate Platinum(II) Compound. Int J Mol Sci, 20:-, 2019 Cited by PubMed Abstract: Stable five-coordinate Pt(II) complexes have been highlighted as a promising and original platform for the development of new cytotoxic drugs. Their interaction with proteins has been scarcely studied. Here, the reactivity of the five-coordinate Pt(II) compound [Pt(I)(Me) (dmphen)(olefin)] (Me = methyl, dmphen = 2,9-dimethyl-1,10-phenanthroline, olefin = dimethylfumarate) with the model proteins hen egg white lysozyme (HEWL) and bovine pancreatic ribonuclease (RNase A) has been investigated by X-ray crystallography and electrospray ionization mass spectrometry. The X-ray structures of the adducts of RNase A and HEWL with [Pt(I)(Me)(dmphen)(olefin)] are not of very high quality, but overall data indicate that, upon reaction with RNase A, the compound coordinates the side chain of His105 upon releasing the iodide ligand, but retains the pentacoordination. On the contrary, upon reaction with HEWL, the trigonal bi-pyramidal Pt geometry is lost, the iodide and the olefin ligands are released, and the metal center coordinates the side chain of His15 probably adopting a nearly square-planar geometry. This work underlines the importance of the combined use of crystallographic and mass spectrometry techniques to characterize, in detail, the protein⁻metallodrug recognition process. Our findings also suggest that five-coordinate Pt(II) complexes can act either retaining their uncommon structure or functioning as prodrugs, i.e., releasing square-planar platinum complexes as bioactive species. PubMed: 30691130DOI: 10.3390/ijms20030520 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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